Protein Is Not Protein: Amino Acids, the Starck Factor, and What Your Body Actually Does With What You Eat

In this episode of The Signal, host Andy Feltovich sits down with Dr. Carlene Starck — protein
biochemist, metabolic nutrition scientist, and founder of Starck Science. Carlene holds a PhD in
Biochemistry from Massey University, spent her postdoctoral years at the Hospital for Sick
Children in Toronto, and trained under two of the giants of protein metabolism research:
Professor Paul Moen and Dr. Robert Wolfe. She recently published a landmark factorial model
of amino acid requirements in the Journal of Nutrition — a paper nine years in the making. This
conversation starts with a provocation: the gram of protein you ate and the gram of protein your
body used are not the same thing. And most of what you think you know about protein quality
stops exactly where the interesting science begins.
What You’ll Learn:
• Why protein quality scores like DIAAS are a useful step — and where they stop telling
the story: first-pass metabolism, liver handling, and what ‘utilization’ actually means
beyond the gut wall
• The Starck Factor: the practical conversion rate between essential amino acid
supplements and whole protein targets — and why the ratio is not 1:1
• Glycine — the smallest amino acid and the most overlooked: why the factorial model
found it may have the largest obligatory losses of any amino acid, including the essential
ones, and what that means for glutathione production, methylation, and the real reason
collagen supplementation might actually work
• How amino acids build more than muscle: tryptophan, tyrosine, serotonin, dopamine,
and the cognitive case for protein that nobody is making loudly enough
• Why catabolism is just as important as anabolism — and why resistance training’s most
important job may be the constant remodeling and quality control it runs on your body’s
entire protein inventory
• The plant vs. animal protein debate, stripped of ideology: what the science actually
shows about digestibility, amino acid composition, and why ‘you can get everything from
plants’ is true — with an asterisk that matters
• Fiber: what it actually does (digestive health, gut lining integrity, short-chain fatty acids),
what it doesn’t do (the observational associations are heavily confounded), and why
fibermaxxing may be solving the wrong problem
• Bioactives and phytonutrients — the final frontier: why the colors of your vegetables are
telling you something, why isolating them tends to fail the same way isolating
antioxidants did, and why the answer keeps coming back to the whole food
• The politics of protein: why a landmark model took nine years to publish, how
institutional inertia keeps outdated requirements in place, and what actually has to
change for the science to catch up with the evidence
If you’ve ever tracked protein grams without asking what your body does with them — or
wondered whether the plant-based protein on your shelf is doing what the label implies — this
episode will change how you think about the question. The science is more complicated than
the guidelines. It’s also more actionable.
Guest Links:
Starck Science: starckscience.com
LinkedIn: https://www.linkedin.com/in/drcarlenestarck/

Transcript

SPEAKER_00 0:00

Welcome to The Signal, the podcast companion to the only intelligence report in men's health and fitness that tells you what to watch, what to ignore, and why. I'm Andy Feldman, founder and CEO. Every episode, we go deeper than the newsletter. Longer conversations, harder questions, and the stories behind the data. We don't do pro science, we don't do wellness theater, we question everything except questioning. Every dogma on trial, guilty until proven innocent. If you're new here, the signal has been produced by Andy Peltman, the flagship company of the Collegium of Order and Flow. Subscribe to the newsletter at the hypensignal.us. Don't forget the hyphen. If this episode is worth five stars to you, leave a review. It's the single best thing that you can do to help us cut the noise. Now let's get into it. Today we have Dr. Carlene Stark, protein biochemist, metabolic nutrition scientist, and founder of Stark Science, where she translates cutting-edge nutrition science into real-world tools and strategies for consumers, health professionals, and food companies. This is for informational purposes only and should not be interpreted as medical or nutritional advice. Carleen, welcome. It's a great privilege to have you today.

SPEAKER_01 1:26

Thank you so much. I'm actually really excited to be here and looking forward to it.

SPEAKER_00 1:32

So let's start at the beginning because I always think the origin story is important where the real interview lives. So you've got a background that doesn't follow the standard career arc of PhD, structural biochemistry, uh postdoc, children's hospital working with prion proteins. So if you could just walk us through your your Batman, Batwoman origin story, as it were, and uh tell us how you got to where you are today.

SPEAKER_01 2:00

So yeah, it's not it's not the normal uh trajectory. Um I mean most academics they do their PhD, they stay on for a bit, do a postdoc, go somewhere else, do another postdoc, end up working in the same area, coming on, um associate professor, professor sort of thing. So um I've never really done things in a normal manner in my life, but uh there is one sort of I guess uh you know common thing that threads throughout everything. And the big one is just a love for protein and a love for brand for protein biochemistry, and so that really started in my undergraduate years. Um so I ended up I went to uni because I originally wanted to be a vet. I love horses, love animals, that sort of thing, and I thought being an equine vet would be super cool until I realized one day working on a farm that I was kind of more interested in what was going on inside the animal than actually helping the animal to survive, which sounds a little bit morbid, but um, it was kind of a key realization. So I ditched the vet thing, but I stayed inside. Um and so it's uh it was my second we're getting are you getting feedback?

SPEAKER_00 3:18

Not on my end, it sounds clean and we'll filter uh we we can edit out any sound issues, so I don't think it's a problem.

SPEAKER_01 3:27

That's good, just to make sure we're not getting it. Um so second uh semester, second semester of Mathusio Uni, I had the best biochemistry lecturer in the world. His name was Stan Moore, he's now at the University of Saskatchewan in Canada, so just in case he's listening, Stan, you're awesome. Um he really instilled for me a real love for protein biochemistry. I'm not really interested in carbohydrate, not really interested in fat, but um he really sort of instilled that he had a great love for it and passion, I think that went on and primarily structure, protein structure. And so then I did my PhD in protein structure, looking at a protein called myostatin, which is actually a really important protein when it comes to muscle growth. So it sort of acts as a bit of a break for muscle growth, and so the thought was at the time that if we could work out what the structure of myostatin is, we can work out how to inhibit myostatin and therefore allow muscle growth to you know ensue, especially in people with, say, muscular dystrophy. Um, so that was sort of the whole thought behind it, and then that PhD didn't go according to plan. Um the structure of myostatin is extremely complicated, and so I was not successful in doing that, but along the way it sort of serendipitously went in. I found out that myoscatin could actually misfold into this amyloid-like structure. So, for those who don't know, amyloid protein is a key protein implicated in Alzheimer's disease, and it seems to, it sort of has a normal structure and a normal function in the body, but for some reason it unfolds and then refolds into into this sort of aggregated form that eventually forms long, long, long fibrils, and these are the things which are found aggregated as parts in the brain of people with Alzheimer's disease. So I found that myosating could be the same thing, and that sort of led me down the prion route. But I think, and then over time, obviously, um I suppose I should finish that story, um, led me down the prion route. When I was in Canada, so I was doing my postdoc in Canada, I got very heavily into mountain biking and competitive mountain biking and became an endurance athlete in that sport. And I sort of realized that what I really wanted to do is take my research, instead of sort of circling around in a lab and academia, and apply it in the real world, especially apply it to uh exercise physiology, athletic performance, that sort of thing. Um, and when I came back to New Zealand, I got a position at Massa University working in exercise physician in an exercise physiology lab. Um, and so sort of more focusing on that. It was a really tough economic time when I came back to New Zealand, so it was kind of it was a mixture between just doing like following what I wanted to do. I actually marched up to the head of the exercise physiology department and said, I'm really awesome, you should give me a job. And he was like, Oh, okay, well, since you think you're awesome, maybe you are awesome and and I'll find some money for you somewhere. Um I think there's a saying which is um sometimes detours in life take you to the best destinations or something like that. And my life has very much been been that kind of path. Um, another one of my very good uh one of the good influences in my life over time uh was the head of department when I was doing my PhD. His name was Jeremy Hyams, and he actually said to me, Carleen, the um sometimes the best career decisions you make are the ones that you don't plan. And so I sort of held on to that, I think. Um But anyway, I came back to New Zealand when I was doing exercise physiology, the money ran out, I didn't know what to do. And so I had put my CV into a whole bunch of different institutes, saying, you know, look, I'm open for work. And uh Professor Paul Moen contacted me and said, I think you'd be really, really awesome for a project coming up that I've got, and it's mathematical modelling. And I was like, I have absolutely no idea what mathematical modelling is, I don't know how to do that, and he said that's okay, I think I think you'll learn. So like, okay. So I jumped into that, and that pretty much took me, um, took me to the rest of of where I am now. So a focus on protein and a focus on nutrition. I was never really that interested in nutrition before, apart from nutrition that's gonna you know support my athletic performance. Um, I had some pretty stuffed up ideas about nutrition, to be honest. I was very much um at the time, I think I was trying to follow the keto diet because that's what I'd heard was really good. Um so I was along the similar lines to what I'm doing now. But anyway, I started this um postdoc with Paul Moen, and and that sort of led into this massive focus on protein and amino acid metabolism where I was it really felt quite sterendous, and then I started with protein, and now I was backworking in protein but in a different way. And so to tie all this together, what I'm what I'm really focused on now is amino acid requirements, and the reason why that's important is actually because of protein structure, so it does fit together. Why does that matter? So if we think about protein structure, one of the most fundamental things you learn in undergraduate biochemistry is that every protein has a structure, and that structure is essential for its function. Protein cannot work properly without its three-dimensional structure in the specific way. So if you think about, for example, um hemoglobin, right? There's there's four hemoglobin molecules that come together, and they have to hold an iron sort of um an iron uh an ion iron, Ion, in their centre so that that can bind to oxygen so that that can be carried around the body. So if those, and that's a three-dimensional structure, if they don't fold properly, they can't come together, they can't hold on to the iron, and they can't bind oxygen. So we don't have any oxygen. Um anyway, so but effectively that three-dimensional structure is uh predicted by its amino acid sequence. So there's 20 different amino acids, and each structure has a unique composition and sequence of amino acids that have to come together in the right way to make that structure. So if we take a step back and we think, well, what do we actually need to eat? We need to eat protein because we need to get amino acids. There's a specific amount of each essential amino acid that we need that is going to allow every single protein.

SPEAKER_00 10:23

So Carlene, uh sorry to interrupt you, but now we are starting to get a bunch of feedback. It's re it is recent, so whatever you're doing, so something changed. Um not sure if we have any options, microphones, headphones, etc., to prevent that feedback.

SPEAKER_01 10:43

I don't have any way of doing it. Would it help if I got headphones? It'll take me a little while.

SPEAKER_00 10:51

A little while by b meaning I need to connect them to my Ac Actually, yeah, that that's that's fine if if you um if yeah if you if you don't mind, and shame on me, I should have mentioned that earlier. That always makes a difference.

SPEAKER_01 11:54

Oh actually I think it's gonna be difficult because I need to do it in a different way. Um just are we still getting feedback now?

SPEAKER_00 12:07

This is it appears to ha be resolved at least for the moment.

SPEAKER_01 12:12

Shall we just cause I'm gonna need to it's gonna take longer because I forgot that these ear pods are um uh tricky and I need the case and I'll probably need to look up how to do it because it's okay.

SPEAKER_00 12:26

Well we we can um we can d drive on for the moment and hopefully we'll be able to edit it out and uh post-production. All right.

SPEAKER_01 12:36

Do you want me to go back to anything?

SPEAKER_00 12:39

Uh so we uh we we can truck on. So I was just uh gonna gonna say that uh uh ra kind of wrap up this section. Uh say you know great great points on protein uh quality, and we're gonna uh come back to that and probably add in uh some comments about three-dimensional structure. So I'll go I'll go ahead and lead in with that and I'll just have my editor uh start here.

SPEAKER_01 13:03

Sorry about it.

SPEAKER_00 13:04

Yeah, no worries. Well, thank you, Carline, for that excellent summary of your background, and I'm I'm glad you point uh pointed out the importance of three-dimensional structure. We often forget that we're three-dimensional creatures that live in a three-dimensional world. I remember the thalidomide, the issues with that, and then caught it was caused by the, of course, the optical isomer uh issue that it was just because it's the same uh compound, how it's arranged in space makes a difference. So we're gonna come back to protein structure, spend a lot of time on that. But I want to go back to your your your mentors and the training you've had because I've always stressed the importance uh that to be the best you have to train with the best, train under the best, and and you certainly did that working with uh several of the giants of protein metabolism. So please talk about those mentors that you studied with, studied under, and how that shaped you.

SPEAKER_01 14:06

Yeah, I I love what you say about if you want to be the best, you have to train with the best, because that's also the story that happened um when I was mountain biking, and I attribute that I attribute my mountain biking success to that specific thing. Um I was riding with World Cup riders and and things like that, and so it just completely changes the way that you think about things and what's possible. And um Paul Moan was actually I had no idea who he was, and so when I started working with him, um it was it was quite a big sort of shock to the system, and then he said to me, probably in my first couple of weeks of my postdoc, oh look, I've got this really good colleague, he's coming over. I think you'd really get on with him. I'd love if you could sit down and have a chat because we're gonna do some work together. And this was Robert Wolfe, who is, as you say, sort of one of the giants of protein metabolism. Again, I had no idea who this person was, so he comes over and sit down and have this fantastic conversation uh with Bob about all things protein, learned probably three or four years of of study in an hour conversation. Um and he was also heading off to the gym after our conversation, which was which was quite cool. Um but I think the biggest thing is that Paul really changed how I think he changed the way that I think about science about how much detail we need to go into in order to fully understand the science. Paul has a very uh goes right into the detail, picks everything apart. If we want to understand something, we need to know every single little thing about it, which is kind of that mathematical modeling approach. Bob, on the other hand, is more in the physiological uh sort of output. He's gotten a huge amount of knowledge in and was actually one of the founders of the isotope tracer methodology, which very much is at the molecular level, but we're more interested in if we put these inputs in what is the overall response. And so what that did is it gave me a really good understanding about what happens when we eat protein, gets digested, what happens in the body, and then what that physiological response is. Um, so I think it gave me a really, really well-rounded understanding of all of that. And so it's quite good because now I'm uh sort of Bob's semi-retired, I don't know if anybody ever retires, Paul semi-retired, and now I'm doing collaborative work with uh Dr. David Church, who is the sort of successor of Paul. So we're trying to keep that relationship and that um that output going. I don't think we'll be, you know, we big, big, big shoes to fill. I'm not sure we'll be able to fill them completely, but oh have have faith in yourself.

SPEAKER_00 16:53

So Dr. Church, uh Dr. David Church, for those of you who don't know, another uh emerging giant in the field along with you, Carlene. So don't be don't be modest. You're going to uh we fully trust you to carry the torch. And speaking about the importance of of good training, I think a lot of your success has also been due to your training in fundamentals, so molecular biochemistry. And that's something like especially me coming in as an an outsider. I just I'm a diligent study, but I just don't have that training in blocking and tackling fundamentals. So and you mentioned uh you you mentioned the import how Dr. Wolf likes to know whatever likes to know that every electron, proton, neutron, subatomic particle is accounted for. So tell us about the importance of that uh training in basic sciences and how that helped you in a in your career.

SPEAKER_01 17:52

Yeah, I'd I I agree. I think that is really important. One of the things I think there's a real disconnect, um, and actually I think I can bring in another level as well. So there's a disconnect between let's say we're talking to dietitians or nutritionists. They're like, eat these foods, get this response. Awesome. Um, calories in versus calories out, focus on macros, that sort of thing. Whereas the molecular biology asks, okay, but what's actually happening in the body to create that response? And not so much even what's happening at the sort of um blood marker level or tissue level, but what's actually happening in the cells. Because if we can understand that, then we can understand the bigger picture. The other part of it is of course having that awareness. I I think one of the things that I've always found with biochemistry, and and I used to tutor a lot of students coming through, and there was a really clear picture between those people who did well at biochemistry and those people who didn't. And it's the ability to think in the grey area. So a lot of people are very black and white, have a protein, have this outcome, have two proteins, they people have this kind of perception that I've got two proteins, they're in the body, they come together, they do a thing. Whereas actually, what happens is you've got a massive globular mess of liquid and all these molecules going around it, and two proteins that may interact, for some reason they just get close enough, and then there's enough of an attractive force that they might you know um attract long enough for a second for that reaction to occur. It's very random and yet extremely elegant. And so when you start to understand that that nuance that's actually happening in the body, it gives you an appreciation of the nuance that actually happens in the diet and the context. And so I think that's that missing piece is the stuff that happens in the middle, how we get from input to output. Um the other part of the thing is, of course, the other thing is, of course, um is it it extends to what we're doing in our research and the findings that we get in our research, how does that actually apply in the real world? There's that disconnect as well, because that's not the same. A randomized control trial is highly controlled, and we and we can start to establish a causal effect from a randomized control trial. We know that if we apply this intervention or this much protein, we get this outcome. But at the same time, that's still in a controlled setting. So, how does that work in the real world? Which is another layer of nuance and context. So I I just think that's the that molecular biology understanding allows you to hold a massive amount of complexity and uncertainty and chaos in your mind at the same time, whilst still allowing there to be some things that we can measure.

SPEAKER_00 20:48

Yeah, that that's a fascinating point. It reminds me of my introductory thermodynamics class when they said there's nothing theoretically to prevent all the molecules in the room from coalescing in one corner of the room and uh and starving us of oxygen. But yeah, it's just in although it's random and chaotic by the miracle of of statistics, we can uh we can channel we can channel the chaos into sensible conclusions. So you mentioned um under understanding the life of the amino acid. Let's w walk us through that because everybody just talks about uh digest digestion and absorption and the story stops there, but there's a there's a lot that goes on um in the life of an amino acid. So walk us through that.

SPEAKER_01 21:40

Yeah, so there's a I um in the recent paper that we published um earlier this year, there's quite a good figure in there sort of talking about talking about that. Although it may not be that interesting of a figure to to the you know general population, but um effectively you know, I think a lot of people think I'm going to eat this protein. The protein's going to get digested into amino acids. They're going to go into my bloodstream. Then they're going to go to the muscle and I'm going to build muscle. Whereas in reality, what you have is you have, I'm going to eat this protein. It's going to get digested into amino acids. Depending on the composition of that protein, some of those amino acids might not make it to the body. The amino acids that make it to the body then have to kind of get through this, like, I don't know, rite of passage, which is the splank mac area, which is also referred to as first past metabolism. So it's the gut and the liver, these organs that have massive requirements for protein and energy. And they kind of get first dips at those amino acids. And so there's a bit of a loss that happens there. And based on the best data that we have available, that's kind of on average around 30% of the amino acids that are digested and absorbed into the body, about 30% of those, probably more by the time we account for protein synthesis, but about 30% of those will be lost. It's not really a loss because the body needs them and it uses them, but 30% are not going to make it through into the sort of peripheral metabolism, into the bloodstream that's going to take them to the different areas of the body, including the muscle. So that's kind of quite a big loss. Once it gets to the muscle, of course, then it can enter protein turnova. And protein turnova is this constant cycle of breaking down protein and then building it back up, and then breaking it down and then building it back up, and then breaking it down, and just goes around and around and around. Now, this isn't just happening in the muscle, it's happening over the entire body all of the time. You've got thousands, tens of thousands, hundreds of thousands of different proteins in the body, and each one of those has a different rate of turnover. So they're all working in different at different rates, but it's constantly happening all the time. And so most, like as I said, most people think about muscle, so we can focus on that. Um the the dietary amino acids that make it into the muscle, they want to get pulled into protein turnover so they can help um keep that thing going and um and amp up the rate of protein synthesis. And so when we're looking at research and we're talking about the ability of a protein to have an anabolic response, that's what we're talking about. How well can it sort of boost that rate of muscle protein synthesis? Um, but of course, this is happening all over the body as well. So some studies that we look at might measure whole body protein synthesis, which is the entire the response of the entire body. Um but then we have lots of other roles for an amino acid. So that's sort of the major role. Those two things that I talked about, the muscle the protein turnover and then the sort of losses that happen in the first past metabolism. Those are kind of two major roles. Um then we have roles in things like neurotransmitter music. So your neurotransmitter serotonin, which is the one that people attribute to mood, precursor to that is actually tryptophan, which is an essential amino acid. And your neurotransmitter dopamine, which most people should be very familiar with now, the precursor to that is tyrophine, which is not an essential amino acid, but it relies on an essential amino acid to make sure we've got enough. So these are some just two examples of really important um functions. Um, the other thing that is important to note is that the gut has a huge requirement for amino acids because it's highly active, it's tuning over at a very rapid way at a rapid rate. And we also have quite a significant loss of amino acids into the gut because the gut's constantly pumping enzymes, shedding tissue, turning over very quickly, and a lot of those um amino acids they never get reincorporated, they kind of move through, they might go to the gut bacteria and then they'll get excreted. So we've got huge amounts of like role for all the different amino acids in the body that we need to think about. We can't just think about muscle. We need to think about all the different roles. Other things are here, our skins, nails, um, menstrual fluid, uh, semen, just if I'm allowed to say those words.

SPEAKER_00 26:33

Absolutely, bring it on.

SPEAKER_01 26:34

Yeah.

SPEAKER_00 26:34

Um but you know, I I might get more viewers that way. So yes, please.

SPEAKER_01 26:39

Yeah, all of the different roles in the body. I think it's fair to say that pretty much every single process in the body relies on protein.

SPEAKER_00 26:47

Well, let's let's dig into muscle for a s a second, just because, as you know, it's a subject near and dear to my heart. Everyone talks about local muscle protein synthesis. So there's the kind of the four quadrant model. There's local muscle-specific anabolism and catabolism, the first two, those are the first two quadrants. And then there's whole body anabolism and catabolism, the second two quadrants. And everybody loves muscle anabolism, and you've probably seen me rant about this on social media, because it's easy to do, right? You you have somebody do an exercise, usually a leg extension, because the vastus lateralis is the easiest muscle to biopsy. And then voila, you've got a boring paper that uh exercise and protein stimulates muscle protein synthesis and this. Okay. It's well uh it's it's it's exciting, but after you see uh a a thousand of the same goddamn paper, it gets a little annoying. So tell so so this is going back to the our theme of transitioning from the mole uh from the molecule to the RCT, the randomized control clin randomized uh control trial to the to the real world. So in in the real world, how do we know that we're doing everything that we need to be be doing? Uh l local and local anabolism in the muscle, uh, global anabolism, local catabolism, global catabolism.

SPEAKER_01 28:21

Yeah, so I think it's worth saying that that muscle protein synthesis does seem to correlate really well with whole body protein synthesis. So um so if you're reading a paper and you're seeing that there's um an increase in muscle protein synthesis, you can be pretty sure that there's an increase in whole body protein synthesis as well. But in terms of what we actually need to do, I mean I think this is where, like if we go back to that um what we're talking about with having a requirement for essential amino acids, um, this is where we really need to have an understanding of how much do we actually need to be consuming in order to hit all of those different requirements. Um as well as making sure we're getting in enough energy. So if we if we're wanting to do the right thing, like if we're wanting to grow muscle, if we're wanting to make sure we've got enough protein to supply the amino acids for all of the body, we need to be consuming enough protein in the first place. We also need to be considering the context. So, are we consuming enough for who we are, for what our goals are, for how old we are, for our all of that sort of thing. Um, and then we need to apply a stressor, such as resistance training, um, in order to really optimize that annibalism, as you said. I think one of the things we were talking about, catabolism. So, catabolism is the breaking down, annibalism is the building up. And I think we need to make sure that we recognize that catabolism is really important. It's just as important. The reason being is that there's a reason why the body breaks down protein and builds it up and breaks it down and builds it up. Part of that reason is that during sleep, um, we need to be supplying amino acids to the body for all of their different roles. And the the greatest supply of those amino acids is the muscle. Muscle is sort of the greatest reservoir of amino acids. It's not a storage facility for amino acids, but it is a reservoir. So we need those amino acids to be broken down, and then we need to eat protein to supply amino acids the next day to fill that back up. Um, but that breaking down also has a role in maintaining the integrity of the different proteins we have in the body, and sort of that goes back to my PhD work in my first postdoc about protein misfolding. So proteins are misfolding all the time. The the ability of a protein to fold into its three-dimensional structure relies on a number of different things, the right environment, and and mistakes happen all the time. I mean, we're human, right? So mistakes are happening, and we have processes in the body that sense those mistakes, and we're like, for example, there's a little alert that goes off, hey, we've got a misfolded protein, we are going to break that up and chop that down and get rid of it. Um, so that's part of that integrity. If we didn't have catabolism, we didn't have protein breakdown, we would have a greater proportion. This is just one example, a greater proportion of misfolded proteins. And those misfolded proteins, A, can't do their proper job correctly, but B have the ability to wreak havoc in the body. Um, so catabolism is important. And I think this then touches on that exercise thing as well. This is why resistance training is such a powerful tool for overall health. Resistance training increases the rate of both breakdown and synthesis. So we're constantly remodeling our muscle, remodeling our protein all over the body, maintaining its integrity and its health. And I think this is uh Gabrielle Lyons, I think, talks about this quite a bit, the difference between muscle mass and muscle health or muscle strength and muscle health. You know, you can have a lot of muscle, but it might not be healthy muscle.

SPEAKER_00 32:19

That's an important point. It's not it's not about the net amount of muscle, it's also about the the quality, and it sounds like by undergoing resistance training you're not only increasing the net amount, but to also you're constantly remodeling and taking out the trash as it were. I want to get into uh protein quality. It's something that you've really you really opened my eyes on. I kind of I kinda personally I kind of went overboard with just carpet bombing. If you get enough protein i if you just eat a lot of protein and uh get enough of it, then all these other considerations drop off, including quality, which I I still think is true to some extent, but you you really changed my mind that about quality and why quality matters. So please uh walk us through uh how you define protein quality and uh and why it matters.

SPEAKER_01 33:14

Yeah, so protein quality is quite a big conversation, I agree. Um it's very important. So when we talk about protein quality, what we're talking about is how well does a protein, one protein, an individual protein, supply all of the essential amino acids that the body needs at their required amounts after accounting for digestive losses. So, what this means is we eat protein, as I said, not all protein is going to make it into the body, we will have some digestive losses. Of those proteins that make it into the body, what is the composition of that protein in terms of its essential amino acids compared to uh what we know well what have been provided as requirement estimates for each one of those essential amino acids? So the thing about protein quality, so it's got a few limitations. So the the pros are it allows us to directly compare different proteins for their amino acid composition after accounting for digestive losses. The cons are nobody eats only one pipe of protein in their diet. So when we think about protein quality, we're saying how well does a protein supply everything if we were to consume it at the estimated average requirement for protein. If we were to consume what they tell us to consume, how well is the protein doing its job? So so we can compare, but yeah, as I said, we don't only consume one type of protein. So then we have to consider how do different proteins interact, how do different proteins interact with the other components in our food that we eat carbohydrates, fat, fiber? Then we have to say, okay, amino acids are entering the body, that's our protein quality. But what happens in all of those other processes we talked about? What happens during first-cast metabolism? How much actually makes it to the body? How well does a protein actually stimulate muscle protein synthesis? Just because an essential amino acid composition is reaching, is getting through the digestive system, that doesn't necessarily mean that the same composition is ending up on the other side of our gut and liver. There's lots of other processes to take into account. So I think protein quality is a great start, a great starting point, and it allows us to directly compare different proteins for their potential value in the diet. Um, but it doesn't necessarily tell us the whole story about how that protein is being used for its different roles in the body.

SPEAKER_00 35:54

So excellent um discuss excellent clarification on some of the myths and some of the limitations of protein quality as it's under as it's commonly understood. I want to, and this this is my terminology, not yours, but I think you're you're stuck with it, the stark factor. So a practical question that practitioners like myself have have had is when we are recommending essential amino acid supplementation, that is, supplementation with just the essential amino acids as opposed to a whole protein supplement, such as whey, how do we fact that factor that into our daily macro targets, our daily protein targets? Because the intuition is that it's more concentrated than a whole a whole protein, so it's probably not a one-for-one. But then the question is the exact number. So I just based on that paper, the the conversion, the my first conversion was 2.4 grams of whole protein equals one gram of essential amino acids. And then you came back and said, well, external validity, extrapolating, you probably need to throw a buffer in there. So I said, okay, two two for one. One gram of whole protein uh i e equals two grams of essential amino acids. So tell us about the the stark factor and how off base I am.

SPEAKER_01 37:24

Well, I mean I mean it's a good I I don't know how uh how well I can how well I can keep that label, but um if it's your label, that's fine. But um what we're really talking about here is we're talking about how essential amino acids are used in the body. Um because what we have to think about is the fact we don't just have essential amino acids, we also have non-essential amino acids. Okay, so when you eat uh protein from whole food, protein quality is really focused on essential amino acids because these are the essential these are the amino acids the body can't make itself. The body has to get them from the diet, otherwise it's not going to be able to build muscle. It's pretty much commonly thought that as long as you're getting in enough essential amino acids, your body can then use those essential amino acids to make all of the other non-essential amino acids that we need. So that's where that's sort of what you're talking about, is there's some studies that show that as long as we're taking in, if we give some people, you know, just essential amino acids, maybe 10 grams, I think the lowest amount is like 3.6 grams, according to Bob. Just essential amino acids, we will get a robust simulation of protein synthesis. And that's because the body has its own supply of non-essentials, but also if we're missing any non-essentials, the body can convert some essentials into non-essentials. It's a process called transamination. Um, not all the non-essential, not all the essential amino acids can do it, but the majority can. Um in reality, it's not quite that simple because what we're finding out is that some non-essential amino acids may actually be conditionally essential and limiting in certain situations. We also know that the body's really good at sort of making up for any losses. So just because we see a robust stimulation of muscle protein synthesis in the short term, that doesn't mean necessarily that what we're providing is adequate. The body may be pulling amino acids from other areas in order to support that. But if we assume we've got a healthy person, they're getting in enough protein, um, all of their processes are working really well, they're not in any sort of um extreme conditions. We can say that if someone was to consume just essential amino acids at a high enough amount, um, it would supply what the body needs. Um, and so this recent paper that you're talking about suggested that in a perfect situation, that ratio of essential amino acids to non-essential amino acids is around 42% to 58%, 41, 59, 42, 40, 58, that sort of thing, which is where you're um coming up with that stark factor number um of around two to one. That if you wanted to calculate how much amino acid essential amino acids you'd need to actually supply protein, then effectively if you had two times the amount of essential amino acids were um if you had just essential amino acids, then it could supply the extra non-essential that you'd need as long as you consumed enough.

SPEAKER_00 40:38

All right. Well, we talk talk talking coming back to those uh essential amino the um non-essential amino acids and uh how some of them might be more essentially more essential than we initially uh expected. Tell us about uh glycine in the role of glutathione production, everybody's favorite topic right now, glu glutathione, the mother, the so-called mother antioxidant.

SPEAKER_01 41:04

Yeah, so glycine is so from the modeling that we did, uh one of the key findings is actually that we have a huge requirement for glycine in the body. We have a huge amount of different roles, glycine has a huge amount of different roles. So um it's the smallest amino acid, uh, but it's small and mighty, so it does a huge amount of roles. And as you mentioned, um it is one of the components of glutathione. So glutathione is actually a tripeptide, which means it contains three amino acids, and glycine is one of those. Um, so if we don't have enough glycine, we effectively cannot make enough glutathione. It has been suggested that glycine is the rate limiting amino acid for glutathione. So glutathione is the master antioxidant. What that means is that it has the ability to help to combat oxidative stress in the body. So oxidative oxidation happens all the time. It's really important for function. Um, we need it for signaling, we need it for processes. Every time we exercise, we're generating um what we might have heard as free radicals. So um some oxidants and and everything that can go through the body. And these, the reason why they're so important is because they're highly reactive. And so they can stimulate other reactions. But of course, if we have too many of them, this can become a problem because they are highly reactive. So we need to have some kind of system to keep that balance in check. And glutathione is one of those uh things that so when we talk about an antioxidant, that's what it's doing, it's helping to keep that balance. And glutathione is the body's primary way, primary way of doing that.

SPEAKER_00 42:49

And let's dig into another important function of us, if I understood correctly, some of these uh non-essential amino acids. You talked about uh neuro neurotransmitter production. Uh was that that accurate, some of those non-essential amino acids and important both both essential and non-essential is both essential. So one one of the things that I've been uh experimenting with is I I started taking essential amino acids, it uh obviously for muscle growth and recovery. But uh also anecdotally, again, sample size of N equals 1 started noticing some uh co increased uh cognitive performance. Has there been a lot of studies on essential, non-essential amino acid uh supplementation and cognitive performance?

SPEAKER_01 43:38

Well, I'm pretty sure that that uh Dr. Church has some stuff um in the works, so that'll be coming out. Um I mean, I mean there has been some studies, they're not showing anything uh really solid. So there's been quite a bit of research looking at tryptophan supplementation and also um tyrosine supplementation. implementation for for affecting increased serotonin and dopamine production. The tryptophan research is difficult because of course in order to see to have a cognitive effect we have we'll eat something that has to make it through the gut, it has to make it through the brain and then it has to cross the blood brain barrier in order to to affect overall cognitive changes. So that becomes a little bit tricky when we're looking at at um at sort of dietary uh dietary intake. But these things do happen. Sometimes it's a dose thing. With tryptophan it's it's a bigger story because tryptophan has to compete with other amino acids to get into the brain. So that's some of the you know I don't know if if you've heard some of the things around making sure you have enough carbohydrate. A lot of people will say that you need carbohydrate to produce serotonin. It's not quite true but carbohydrate does help to improve um the uptake of peptopine into the brain. I think there's a little bit better research with tyrosine in supporting dopamine um dopamine production and tyrosine is one of the things that can be effective in something like Alzheimer's disease or um there's also a Cushing's disease which can impact dopamine production. So I definitely um I'm definitely a proponent of taking essential amino acid for needs some non-essentials for cognitive performance. The research is emerging but every single person I've talked to that uses essential amino acids for that purpose um will see beneficial effects.

SPEAKER_00 45:43

Okay. Well hopefully I'm yeah so so hopefully my theory will be uh validated it uh would do wonders for me and my street cr street cred. I've always joked if you're if you're right enough for long enough maybe people will start listening to you but maybe that's also just wishful thinking on my part. I want to uh dig in a little bit more to the the essential non-essential conditionally essential uh distinction because I've a lot of people and I've fallen in this trap have got are under the impression that non essential or conditionally essential means that we don't need to pay attention to them. But it's it sounds like that uh particularly particularly in the case of glycine the rate limiting glutathione uh precursor that it's often difficult to uh that it people are often deficient or at least suboptimal.

SPEAKER_01 46:39

So what do you what do you think about uh supplementing uh with that uh possibly in the form of uh collagen as you've mentioned before in our discussions yeah so there are I've I've played around quite a bit with supplementing with pure glycine um and with collagen um this is one of the things that that I'm sort of tossing up between at the moment is is a lot of people take collagen for you know joint health and and say say that it improves joint health. There's not a huge amount of research behind that that supports that outcome. And you'd I mean if we think about it when we eat collagen the body doesn't eat the digestive system doesn't sort of take the collagen and just absorb it straight away and then it goes to your joints where it's needed or to to your skin. It gets broken down into its constituent amino acids, some peptides and then it has to go into the body and then get remade and so what we're doing when we're having collagen if we're trying to support joint health or skin health or hair or whatever is that we're supplying the the sort of the building blocks that hopefully then will improve um overall synthesis. But one of the like one of the key amino acids in collagen is glycine. So glycine um has a I think it's around 33% or something like that. I could be wrong in pulling numbers out of somewhere in my brain. But it's it's a huge proportion of glycine and so and so for every sort of 10 grams of collagen you consume you might get around three grams of glycine. So my hypothesis if you will is that the a key function of collagen is actually to provide the body with glycine because it is extremely important not just for glutathione plays a big role in helping to balance methylation processes in the body. A lot of people have talked about methylation it's one of the most fundamental pathways in the body methylation supports so many different functions anywhere from DNA synthesis and RNA synthesis through to helping to regulate neurotransmitter production and and breakdown it's also got a huge role to play in cardiovascular health. So the thought is that glycine can also play a big role there glycine also seems to have a uh sort of uh calming effect in the brain um I'm pretty sure it can be combined is a neurotransmitter I think it's GABA could be wrong not a neurologist but um does seem to have a calming effect. The other thing which has been proposed for Glysen is that having it before sleep can actually enhance sleep. So it seems to decrease core body temperature if you take a large dose which is a key factor in supporting sleep. So I think there's a lot of different roles we haven't got enough science to say anything in particular but it's not going to do you any harm um to supplement with collagen for the purpose of the glycine there is some research showing that um in some average healthy people taking additional glycine does improve glutathione synthesis and glutathione status. So I think that's um good evidence that that you could definitely support your health with it.

SPEAKER_00 50:06

Okay yeah I've always been skeptical of the the collagen and and joint health hypothesis one for the reason you mentioned that these collagen you don't actually eat and absorb collagen you eat the raw material and like every other most most every other protein it gets ground down into its constituent parts but I I like your theory about the glycine as a as um all of its other beneficial uh functions beyond beyond glutathione production I think that's very intriguing. Want to uh we could talk about uh especially you could talk about I'm sure you could uh uh talk about protein all day all week but I want to get into another uh trending top topic uh fiber maxing and how fiber is the new protein which is a strange uh which is a strange uh metaphysical possibility uh a physical possibility two things uh being different but the same so if you could walk us through uh fiber maxing the new trend uh what are we actually uh looking for with fiber uh what are people missing so with fiber the the the key argument is really and and I think the reason why people are talking about fiber as a new protein is that the key argument is that people aren't protein deficient but they are fiber deficient.

SPEAKER_01 51:29

And so if we're going to be focusing on anything in the diet the fact that um you know if we look at say if we took NHANE's dietary intake data so the US national um nutrition survey data um and we look at people's protein intake it comes on average it's sort of 1.1 grams per kilogram body weight per day which is greater than the minimum recommendation of 0.8 um as the the RDA. Whereas most people with fibre the recommended intake is around 30 grams per day depending on your age, your sex etc whereas people are sort of around the 15 grams about half that amount so because people are consuming so little fibre we should be focusing on fibre. The other part of this is of course that there's a huge amount of research supporting fibre for health outcomes cardiovascular disease so as we increase fibre intake we see decreased risks for cardiovascular disease type 2 diabetes mortality cancer all of those things so we know there's a beneficial relationship between fibre and health we know that people aren't eating enough so let's tell people to eat more and more and more and try and improve health but this is something this is the way that that nutrition seems to work in nutrition science people like hey there's this awesome health outcome there's this one nutrient that seems to do these things let's jump on it let's shove it down everyone's throat the same thing happened with protein um that doesn't mean we should be putting protein into chips and ice cream and and everything right like let's tell people to consume protein in a healthy way but that's beside the point I mean fiber is never going to be the new protein because they have completely different roles in the body and I have a slightly neurodivergent brain and when I hear fibre is the new protein I'm like it doesn't even make sense who came up with that. It's just not scientifically possible. But um but I can see where they're going at what they're trying to do is trying to say fiber is a new protein in in terms of the new thing that we need to be focusing on and trying to up that I have some issues with fiber and I've thought about it quite a bit wondering whether it's actually as important as what everybody makes it out to be and this is just my personal usings. It's not based on anything um you know like it's definitely based on on the evidence but the sort of thing that keeps me up at night. Because we have all these people that are on the keto diet and the carnival diet whose fiber intake is probably I mean on the carnival diet you've pretty much got zero grams of fiber. On the keto diet you're probably lucky to hit that 30 grams and yet we're not seeing any massive negative effects yet from those diets. There's been a few things come out you know um unhealthy gut markers and so on but we're not seeing any really negative health outcomes and we know that it improves metabolic status quite a lot quite effectively. And yet on the other side of the coin you've got all these you know people on probably plant-based diets we see positive effects and what I'm wondering is when we're looking at fiber intake and epidemiological research so we're looking at the entire diet we're not just looking at fiber we're looking at everything else that comes with that fiber primarily bioactive compounds and plants which also have been shown to have the same effects on health as fiber reduced risk of cardiovascular disease reduced risk of cancers you know um reduced risk of type 2 diabetes all of that kind of thing so I don't know if we can attribute all of the health effects to fiber what we can attribute really strongly to fiber is digestive health. And there's a lot of you know if we look at randomized controlled trials where we are supplying a fiber intervention it's very very clear that it supports digestive health and um that would be the big outcome that I would suggest may be impacted by things like the carnivore diet and the keto diet downward scale.

SPEAKER_00 55:51

So so let's talk about digestive health for a moment what are we what do we even mean by that when we talk about digestive health yes um how well do we poo um is what most people go through important it is important.

SPEAKER_01 56:06

I mean our digestive system starts in our mouth right really it starts in when we consume goes down our throat all the way out to to our rectum anus um when we excrete the stool but if we think about the digestive system one of the most important parts of it yes we've got the gut microbiome but I would say that further upstream of that we've got our gut lining our mucus layer and our digestive system is sort of it's it is inside us but it's really external to the body because it's uh exposed to the outside world and so that gut lining is kind of a barrier it's like another skin it's a barrier between our our gut and the rest of our body and so the integrity of that gut lining is hugely important. And the gut lining is also the thing that houses our gut microbiome. So to maintain that integrity what we need to do is we need to be as we talked it up with protein turnover constantly breaking it down and building it up and breaking it down and building it up. And fibre has a role in soluble fibre mainly in helping to sort of share that lining and break it down and pull it off so that then protein can be rebuilt. So that's a big role for fibre. The other part is of course we want to make sure that we're moving everything through the body because that helps to maintain a good rate of digestion absorption of nutrients the other part of there seems to be a relationship between fibre intaking and colon cancer and so it does seem to have a role.

SPEAKER_00 57:36

Again I think this may be more to do with potentially bioactors but it does seem to play a role in in reducing that risk and so the health I think that's that's really the health of the gut microbiome and supporting that because the fiber that we that we cannot digest is a substrate for the gut bacteria to consume and then they are part of that consumption is they ferment they sort of ferment the fiber and that produces something called short chain fatty acids among other things which seem to have really good roles in the body when they get absorbed so for me really if we're thinking about digestive health we're thinking about how well does the digestive system actually work in terms of moving things through but how um how sort of robust is our gatlining how what is the integrity of it and how healthy is our gap microbiome yes I'd never thought of that the importance of fiber in that turnover that protein turnover and the lining some analogous to the remodeling that resistance training does in the muscle so very very insightful. Let's let's talk a little bit about uh phytonutrients there's a there was an old joke why do people uh why do people focus so much on macros well it makes for easy math there's only three of them then you want to get into the micronutrients then you've only got a few dozen now we go into phytonutrients b bioactives polyphenols and we've got thousands that we know about and probably more we don't know about many and very few of which we actually understand. So talk about let's uh spend a moment to just talk about that final frontier I hate to say final because I'm sure there'sn't going to be another front frontier but let's talk about the the those bioactives and their importance and what we know about them for a moment.

SPEAKER_01 59:28

Yeah I mean as you mentioned there's a huge amount and there's a lot of people working specifically on them. I think we know the most about the carotenoids to be honest which is the sort of uh yellow orange red colours so um this is the thing which always I get very excited by very basic uh phenomena but um the you know the colours of fruits and vegetables that we eat that colour that we're seeing is actually those um a lot of that is coming from those bioactives because they are a pigment they're a bioactive pigment so when we see yellow or orange or red that's a clear indication that it's got carotenoids and when I say carotenoids I'm talking about things like beta carotene, alpha carotene, um things like that. So and there's quite a bit of research suggesting that there is a beneficial effect of carotenoids on reduced risk of cancer especially skin cancer because the carotens tend to sort of insert themselves into and house themselves in our skin cells and provide protection. Where does that protection come from a lot of those roles are antioxidant roles and we've already talked about antioxidants but they seem to have a huge number of other roles anti-inflammatory anti-tumor they seem to help to prevent the growth of cancer cells one of the big limitations is that most of our research comes from mechanistic studies so looking at animals and looking in cultured cells. We don't have a huge amount in humans and part of the reason for that is because of we seem to have a difference in effect when we supply phytonutrients in their whole food form versus when we isolate them. So they seem to have this synergistic way of working which is really nice but makes it very hard to study. The other um interesting thing is some of them have a bimodal effect where at low doses they're really effective and then at high doses they can become quite toxic because one of the ways they actually work is not necessarily have a direct antioxidant effect but because they are slightly stressful to the body they sort of stimulate the body to increase its own antioxidant effect and then that helps to to mop everything up whereas if we give the body too much of it sort of overwhelms the body's response. So they all work in different ways. The other interesting one is anthocyanins which are a type of polyphenol and you'll get those from things like blueberries black currants and there's a huge amount of research suggesting that these anthocyanins have a role in recovery especially muscle recovery from exercises.

SPEAKER_00 1:02:12

So not not too little not too much and don't try to perfect that which God has already perfected just eat the whole food no you don't need a you don't need a frankin you don't need a franken food functional food. Well never never say never everything has its place. We could of course talk for days but there's one important thing I want to touch on and this gets to the whole um the f whole fight false dichotomy of plants versus animals. When you one of the implications of your research is that protein quality matters and then the debate immediately goes to how do you get pro high quality protein and correct slap me if I'm wrong animal protein is higher quality than plant protein the way we we define it. So how do you how do you counter the um how do you address the false dichotomy the the the war the warring uh feuding pagan diet cults of um carnivore versus vegan and uh and and um and what you're actually trying to communicate with protein quality well that's that black and white thing right we can you know carnival versus vegan is a really good example of either it's one way or the other and it's not it's um they those are two ways of eating I definitely believe that we can obtain what we need in many different ways but if we look at the science and we take a very objective view so there's sort of there's the science and and there's what the science shows what the data show and then there's ideology and our beliefs and how the way that we eat can sort of form a big part of our identity and and we if we really want to understand things we have to keep those separate.

SPEAKER_01 1:03:55

So if we look at the science it's very very clear that animal proteins are higher in quality than plant proteins and that's not because they're they're better in a sort of moral way it's just that the body digests them so much more effectively and on top of that the composition the amino acid composition of animal proteins is much more similar to what the body needs which makes sense we are animals so you would think that other animals would have what we need and the amino acid composition that we need versus plants. Plants or the fibre they have some anti-nutrients in there that seem to decrease the digestibility of plant protein so we just get less into the body and then they have a much lower proportion of essential amino acids in general than animal protein. So those two things together mean that quality is lower how do I put them together I'm very much a I mean if we look at a team a team of people working in an organization a great team has lots a mixture of strength. So we might have someone that's really really ideation ideas creation and going for things. That person is awesome but they're terrible at follow through and implementation so we need somebody to come in that's really good at taking those ideas and making it happen and executing. And then we probably need someone that has the ability to audit what comes out and make sure that the quality is high. So we have all these different roles and that's the way I think about food in the body animal proteins are the most effective efficient especially when it comes to you maintaining a chloride balance way of supplying the body with protein plant foods and plant proteins are great at providing fibre and phytonutrients so in my mind put those things together and you have a perfectly balanced diet that does not mean you can't get what you need from plants. But you have to realize that there's a trade-off. I'm not going to get as much protein or essential amino acids. So I need to eat more. And then that may mean that I need to eat more calories in order to get that protein. So how am I going to balance that out? So I just find that to keep things really simple and outside of the whether I'm a vegan or a carnivore or whatever it is, the combination of animal protein, plant foods to support that protein supports health, uh really, really effectively.

SPEAKER_00 1:06:40

Yeah, you're absolutely right. It's so hard to separate science from identity. And I've I've struggled, struggled, grappled with that my entire career just trying to tell people, look, I'd do it do whatever you want, vegan, vegan carnivore, whatever. I'm just trying to objectively communicate what the data say. Unfortunately, all good things must come to an end. So we're coming up on the the lightning round. What's the most overrated nutrition trend you'd like to see go away or at least stop hearing about?

SPEAKER_01 1:07:13

I'm gonna get in trouble here. But it would be what we're just talking about, which is probably uh I don't want to say veganism because I know that there's the there's that belief aspect, but probably the the plant-based being the way to go. Um purely because of the science.

SPEAKER_00 1:07:31

Absolutely. And again, it's worth re-emphasizing. If got God outranks me, if you're or it even if for ethical convictions, if if that if that's what your conscience tells you to do, great. But when you try to when you try to mask it with in science, that's when I have a problem. If you could fix uh one thing about how protein research is communicated to the public, what would it be?

SPEAKER_01 1:07:54

It really is that that focus on um protein as an amount and communicating the amount of protein moving into talking more about amino acids. I think that people need to understand that protein, we don't eat protein for protein, we eat protein for amino acids. What does that actually mean and how do I obtain those?

SPEAKER_00 1:08:15

Alright, and last and final uh personal question what advice would you give to your younger self if you could talk to her?

SPEAKER_01 1:08:24

So it's an interesting question because I actually um have talked to quite a few, given a few talks to younger people and given them advice. Um and the one that I would say to myself, although I think my younger self was already like this, um but is to always challenge the straight the status quo. So I think it's very, very easy. I mean, you know, I had some great some great re uh mentors and researchers and and ongoing collaborators, and the reason why they're so great is because we could have conversations where I could challenge them. Sometimes I'm wrong, and they're like, no, this is the reason why. Okay, that's great, but they were always open to that, and I think um we always need to learn how to stand back and and look at the data, question it for ourselves, investigate, um, and figure out what works for us as opposed to constantly just following whatever the latest trend is.

SPEAKER_00 1:09:17

Absolutely. I I'm glad you brought that up. It's you should never always ask the question, don't assume somebody's thought thought of it before. And I'm talked a little bit about this offline, some of the things I'm coming up I'm stumbling on with third-party testing, finding out that just nobody's asked these questions before. And when you start asking questions, you get some pretty frightening answers. So more on that.

SPEAKER_01 1:09:41

Knowledge evolves, right? We can't just we we don't sort of learn something and then that's it. Um if you look at the the literature now compared to what it was 20, 30 years ago, some things still hold, some things have completely changed.

SPEAKER_00 1:09:54

So absolutely. And before we part ways, the listener who wants to learn more and follow you. I know you're active on LinkedIn. Uh if you're if you're not qual uh currently following uh Dr. Stark, you need to get on it. Uh, what else should our listeners be doing?

SPEAKER_01 1:10:12

So one I've kind of got um so many things on the go. Uh I've got a website um which is Stark Science, so S T-A-R-C-K-Science.com that is currently under, it's getting updated, um, but uh hopefully soon. Uh one of the things that I'm actually doing is I've I've built a uh uh protein quality calculator, which is gonna be on that site, so you can go in and and uh play around with your diet and figure out what the protein quality is and we'll give you a give you a report on that. So I'm excited about that to put that on the website. Um I am going to be starting a YouTube channel. That's one of my to dos, but probably the best way to follow me at the moment is LinkedIn.

SPEAKER_00 1:10:52

Great. Well, again, Dr. Stark, it's been a great honor to host you and look forward to hearing more from you.

SPEAKER_01 1:10:58

Thank you so much, Ron. Thank you.