Protein Guru

Whenever I read the top level research on Protein I keep running into one name – Dr. Donald K. Layman. (His Twitter feed). Here’s some of the studies he has been a part of on the subject of Protein:

I didn’t realize he is in a video lecturing on Protein:

This video is well worth an hour. Key concepts are distribution, amount, timing, quality of protein. Takeaways:

  • It takes about 30 grams of protein in a meal to lead to Muscle Protein Synthesis (MPS). Less than 20 grams of protein on a meal have no effect on MPS. Never eat less than 30 grams of protein in a meal.
  • You are catabolic until you eat protein (breakfast or when you end an Intermittent Fast).
  • Eat at least three meals with greater than 30g of protein per meal.
  • Eat high quality protein with enough Leucine (at least 3g) at each meal
  • Eat protein first then carbs afterwards.
  • Protein burns more energy – commonly attributed to the Thermic Effect of Food -which is the action of MPS. Building muscle burns energy.
  • MPS peaks at 90 mins and is back down to baseline at 180 minutes.
  • MPS eventually declines due to a drop in ATP (energy).
  • Protein accelerates the gain from exercise.
  • Snacks tend to be carbohydrates (without Protein) and lead to fat gain.
  • Skipping breakfast isn’t good. I accommodate this by breaking my fast later in the day (intermittent fasting). I eat at 11:30, 2:30 and when I get home in the evening (typically 5:30 to 7:30). This makes me catabolic about 13 hours a day (10:30 PM to 11:30 AM) and anabolic for 11 hours a day (11:30 AM to 10:30 PM).
  • Reduce carbohydrates to less than 30 grams per meal (I try to do much less than that).
    • Total carbs divided by total fiber < 6 – eat whatever you want.
    • Eliminate food which has carbs divided by total fiber > 10 (bread, grains, etc).

Meals (Using his concepts)

Meets goal of at least 3 grams of Leucine.


  • 4 hard boiled eggs, 4 slices of bacon
    • 36g protein, 32g fat, 2g carbs, 460 calories


  • 128g Chicken Breast, boneless/skinless
    • 39g protein, 6g fat, 0g carbs, 220 calories
  • 3 medium sized chicken drumsticks
    • 47g protein, 17g fat, 1g carbs, 358 calories
  • 165g Pork Ribs
    • 38g protein,  31g fat, 0g carbs, 479 calories
  • 120g Colby Jack Cheese
    • 31g protein, 41g fat, 2g carbs, 500 calories

Vegetable/Nuts/Fruits Carbs to Fiber Ratios

Carbs with ratios less than 6 are ad libitum (eat as much as you want):

  • Flax Seeds (30g serving) – 8.7/8.2 = 1.06
  • Chia Seeds (1 Tablespoon serving) – 4.2/3.4 = 1.24
  • Mushrooms (85g serving) – 2.8/1.9 = 1.47
  • Cabbage (1 cup) – 7.6/4.7 = 1.61
  • Cauliflower (85g serving) – 4.2/2.5 = 1.68
  • Kale (85g serving) = 7.4/4.4 =  1.68
  • Almond Flour = 5.9/2.6 = 1.79
  • Blackberries (1 cup serving) – 13.8/7.6 = 1.82
  • Asparagus (85g serving) – 3.5/1.8 = 1.94
  • Radish (85g serving) – 2.9/1.4 = 2.07
  • Broccoli (85g serving) – 4.5:2 = 2.25
  • Lettuce Mixed Greens (85g serving) – 2.7/1.1 = 2.45
  • Spinach (85g) – 3.1/1.2 = 2.58
  • Zucchini (medium – 196g) – 6.1/2.0 = 3.05


Gaining Muscle During a Cut

Leucine seems to be the central amino acid in muscle protein synthesis.

There’s plenty of interest in gaining muscle while cutting fat. Here’s an interesting item from a paper on that subject (Donald K. Layman, Jamie I. Baum. Dietary Protein Impact on Glycemic Control during Weight Loss. The Journal of Nutrition, Volume 134, Issue 4, 1 April 2004, Pages 968S–973S):

During catabolic periods such as energy restriction, supplementation with leucine or a complete mixture of the 3 BCAAs, leucine, isoleucine, and valine, stimulates muscle protein synthesis (35-37).


The three references (35-37) are:

35. Li, J. B. & Jefferson, L. S. (1978) Influence of amino acid availability on protein turnover in perfused skeletal muscle. Biochim. Biophys. Acta 544:351–359.
36. Buse, M. G. & Reid, S. S. (1975) Leucine. A possible regulator of protein turnover in muscle. J. Clin. Invest. 56:1250–1261.
37. Hong, S. C. & Layman, D. K. (1984) Effects of leucine on in vitro protein synthesis and degradation in rat skeletal muscle. J. Nutr. 114:1204–1212.

All three were rat studies. From 36.

The data presented indicate that leucine may act as a regulator of the turnover of protein in muscle cells. They are compatible with the hypothesis that leucine inhibits protein degradation and promotes protein synthesis in muscle.

Human Studies

Lundholm K, Edström S, Ekman L, Karlberg I, Walker P, Scherstén T. Protein Degradation in Human Skeletal Muscle Tissue: The Effect of Insulin, Leucine, Amino Acids. Clin Sci (Lond). 1981 Mar;60(3):319-26.

Satoshi Fujita, Effect of insulin on human skeletal muscle protein synthesis is modulated by insulin-induced changes in muscle blood flow and amino acid availability  Am J Physiol Endocrinol Metab. 2006 Oct; 291(4): E745–E754.

Changes in muscle protein synthesis were strongly associated with changes in muscle blood flow and phenylalanine delivery and availability. In conclusion, physiological hyperinsulinemia promotes muscle protein synthesis as long as it concomitantly increases muscle blood flow, amino acid delivery and availability.


Protein is not insulinogenic

In other words, Protein has minimal effect on your Insulin levels (Donald K. Layman Jamie I. Baum. Dietary Protein Impact on Glycemic Control during Weight Loss. The Journal of Nutrition, Volume 134, Issue 4, 1 April 2004, Pages 968S–973S.):

These data suggest that amino acids have minimal impact on plasma insulin concentrations when entering the body via the GI tract.

There’s data which shows a large effect of protein on Insulin but that protein was mainlined into the veins of the test subjects. Unless you are injecting your protein, you’ve got nothing to fear from protein.

Most of these studies used direct intravenous infusion of amino acids into the human forearm under fasted conditions and used euglycemic clamp techniques to measure glucose uptake and insulin resistance. Using these techniques, investigators found that acute increases in plasma amino acid concentrations resulted in higher plasma glucose concentrations, lower glucose uptake, and elevated plasma insulin levels.

Here’s one experiment cited which makes that point:

One of the first studies of the differences in amino acid metabolism between i.v. administration and oral intake was by Floyd et al. (51,52). These investigators evaluated the insulin response to i.v. infusion of amino acids or glucose (51) and also examined the insulin response to oral intake of protein (52). They found that infusion of 30 g of amino acids produced a 3-fold higher insulin response (∼180 μU/mL) than infusion of 30 g of glucose (∼50 μU/mL), suggesting a dramatic hyperinsulinemic effect of amino acids.

However, these investigators also examined the same measurements after subjects consumed a meal of 500 g of beef liver and found that the peak insulin response to the protein meal was only 30 μU/mL. Assuming that leucine is 1 of the most potent insulin secretagogues, the i.v. infusion provided <5 g of leucine while the beef meal provide >14 g of leucine (52). These data suggest that amino acids have minimal impact on plasma insulin concentrations when entering the body via the GI tract.

BCAAs may be the exception since the reach the bloodstream directly like carbohydrates…

The primary exceptions to this pattern of modifications are the BCAA, with over 80% of dietary content of leucine, valine, and isoleucine directly reaching blood circulation.

I wonder if that’s part of their popularity as a supplement?

Speed has an effect too:

For glucose, the postprandial handling occurs mostly within the first 2 h (43); however for amino acids the rate of disposal is much slower with <20% of the dietary amino acids degraded within the first 2 h (48). Thus, direct comparison of a high carbohydrate diet vs. a high protein diet is that the carbohydrate diet requires rapid equilibration of the glucose and insulin metabolic system with dramatic shifts between hepatic vs. peripheral regulations, while a high protein diet serves to stabilize the glycemic environment with delayed metabolism and less reliance on peripheral insulin actions.

And most relevantly to this page:

…diets with reduced carbohydrates and higher protein stabilize glycemic control during weight loss

This part gets really interesting since it describes metabolically broken folks like us…

As expected, as the subjects lost weight (∼6.3 kg) during the 10-wk energy restriction and they improved glycemic control as measured by reduced postprandial insulin response to the test meal. For the CHO Group, average values at wk 0 = 77 μU/mL and at wk 10 = 38 μU/mL. On the other hand, subjects consuming the moderate protein diet achieved normal values for 2-h insulin response after only 4 wk on the diet with average values at wk 0 = 75 μU/mL and at wk 10 = 12 μU/mL. These changes appear to be beneficial associated with the overall risk patterns of obesity and Metabolic Syndrome (57,58).

In summary:

In summary, use of diets with higher protein and reduced carbohydrates appears to enhance weight loss with greater loss of body fat and reduced loss of lean body mass. Beneficial effects of high protein diets may be increased satiety, increased thermogenesis, sparing of muscle protein loss, and enhanced glycemic control. Specific mechanisms to explain each of the observed outcomes remain to be fully elucidated. We suggest that a key to understanding the relationship between dietary protein and carbohydrates is the relationship between the intakes of leucine and glucose. Leucine is now known to interact with the insulin-signaling pathway with apparent modulation of the downstream signal for control of protein synthesis resulting in maintenance of muscle protein during periods of restricted energy intake. Leucine also appears to modulate glucose use by skeletal muscle. While total protein is important in providing substrates for gluconeogenesis, leucine appears to regulate oxidative use of glucose by skeletal muscle through stimulation of glucose recycling via the glucose-alanine cycle. These mechanisms appear to provide a stable glucose environment with low insulin responses during energy-restricted periods.



Are the Protein RDA Values Enough?

A metabolic unit study was performed to determine the effects of eating higher protein levels than the RDA and weight loss. (Pasiakos, S. M., Cao, J. J., Margolis, L. M., Sauter, E. R., Whigham, L. D., McClung, J. P., Rood, J. C., Carbone, J. W., Combs, G. F., Jr., Young, A. J. Effects of high-protein diets on fat-free mass and muscle protein synthesis following weight loss: a randomized controlled trial. FASEB J. 27, 3837–3847 (2013).) The study:

…assessed body composition and muscle protein synthesis responses to controlled diets manipulating protein intake over a range that spans the current acceptable macronutrient distribution range during short-term Energy Deficit (ED).

The study concluded:

…determined that consuming dietary protein at levels exceeding the RDA may protect fat-free mass (FFM) during short-term weight loss.

In summary, consuming twice the amount of dietary
protein than current recommendations measurably
protects FFM and promotes the loss of body fat during
short-term weight loss, likely through the maintenance
of muscle anabolic sensitivity to protein ingestion.
However, consuming dietary protein at 3 times the
RDA does not appear to confer any additional protective


Muscle Protein Synthesis in the Elderly

Here’s a good study/article on Protein and the Elderly (Adv Nutr. 2014 Sep; 5(5): 599S–607S. Published online 2014 Sep 1. doi: 10.3945/an.113.005405
PMCID: PMC4188243. Keeping Older Muscle “Young” through Dietary Protein and Physical Activity. Daniel R. Moore*). One of the points

…35 g (∼0.45 g/kg) of whey protein stimulates mixed muscle protein synthesis in older adults, whereas 10 and 20 g (∼0.13 and ∼0.28 g/kg, respectively) do not.


Individuals who more frequently elicit a maximal stimulation of muscle protein synthesis throughout a daily meal feeding cycle would be more likely to maintain muscle mass and possibly function. This could explain in part the greater retention of lean body mass in older adults who consume more than the current RDA for protein [i.e., ≥1.2 g/(kg ⋅ d)] relative to those who habitually consume a suboptimal amount [i.e., <0.8 g/(kg ⋅ d)]


Muscle Protein Synthesis from Eating Protein

From (Muscle for Life. The Truth About Protein Absorption: How Often You Should Eat Protein to Build Muscle. Michael Matthews):

When you eat protein, your stomach uses its acid and enzymes to break it down into its building blocks, amino acids. These molecules are transported into the bloodstream by special cells that line the small intestine, and are then delivered to various parts of the body. Your small intestine only has so many transporter cells, which limits the amount of amino acids that can be infused into your blood every hour.

The article goes on to say that different proteins sources are absorbed at different rates.

According to one review, whey clocks in at 8 to 10 grams absorbed per hour, casein at ~6.1 g/hr, soy at ~3.9 g/hr, and cooked egg at ~2.9 g/hr.

Here’s a really interesting point that I didn’t know about:

For instance, the presence of protein in the stomach stimulates the production of a hormone that delays “gastric emptying” (the emptying of the food from the stomach). This slows down intestinal contractions and thus how quickly the food moves through the small intestine, where nutrients are absorbed. This is one of the ways your body “buys the time” it needs to absorb the protein you eat.

That seems to be the mechanism by which protein gets processed by the body. That’s how the area under the curve for protein is so long.

The article goes on to say that:

Carbohydrates and fats can move through your small intestine and be fully absorbed while the protein is still being worked on.

The page then quoted a study (Protein feeding pattern does not affect protein retention in young women) which indicated that it doesn’t matter if the protein is consumed all at one time (Intermittent Fasting style) or over the course of the entire day.

It was higher during the experimental period, but not significantly different in the women fed the spread or the pulse patterns [59 +/- 12 and 36 +/- 8 mg N/(kg fat-free mass. d) respectively]. No significant effects of the protein feeding pattern were detected on either whole-body protein turnover [5.5 +/- 0.2 vs. 6.1 +/- 0.3 g protein/(kg fat-free mass. d) for spread and pulse pattern, respectively] or whole-body protein synthesis and protein breakdown. Thus, in young women, these protein feeding patterns did not have significantly different effects on protein retention.



Gaining Muscle on a Low Carb Diet

Two interesting studies.

René Koopman, Anton J. M. Wagenmakers, Ralph J. F. Manders, Antoine H. G. Zorenc. Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects. American Journal of Physiology-Endocrinology and MetabolismVol. 288, No. 4. 1 APR 2005. Concluded:

We conclude that coingestion of protein and leucine stimulates muscle protein synthesis and optimizes whole body protein balance compared with the intake of carbohydrate only.

René Koopman, Coingestion of carbohydrate with protein does not further augment postexercise muscle protein synthesis. American Journal of Physiology-Endocrinology and Metabolism, Vol. 293, No. 3. 1 SEPT 2007. Concluded:

…coingestion of carbohydrate during recovery does not further stimulate postexercise muscle protein synthesis when ample protein is ingested.

These results are in spite of the greater amount of Insulin that is secreted by carbs plus protein.

Or, as Lyle McDonald puts it:

NSAIDs and Exercise Recovery

Here’s why I avoid NSAIDs after exercise (Sports Med. 2012 Dec 1;42(12):1017-28. The use of nonsteroidal anti-inflammatory drugs for exercise-induced muscle damage: implications for skeletal muscle development. Schoenfeld BJ.):

Exercise-induced muscle damage (EIMD) is a common condition resulting from a bout of vigorous exercise, particularly if the individual is unaccustomed to performance of the given movement. Symptoms of EIMD include delayed-onset muscle soreness (DOMS) and a loss of physical function.

Nonsteroidal anti-inflammatory drugs (NSAIDs) are routinely prescribed post-exercise to alleviate these symptoms and restore normal physical function.

Of potential concern for those who use NSAIDs to treat EIMD is the possibility that they may impair the adaptive response to exercise. Specifically, there is emerging evidence that the action of cyclo-oxygenase (COX) enzymes, and COX-2 in particular, are important and even necessary to achieve maximal skeletal muscle hypertrophy in response to functional overload. Given that NSAIDs exert their actions by blocking COX and thus suppressing prostaglandin production, a theoretical rationale exists whereby these drugs may have detrimental effects on muscle regeneration and supercompensation. Therefore, the purpose of this article is to extensively review the literature and evaluate the effects of NSAIDs on muscle growth and development.

Based on current evidence, there is little reason to believe that the occasional use of NSAIDs will negatively affect muscle growth, although the efficacy for their use in alleviating inflammatory symptoms remains questionable. Evidence on the hypertrophic effects of the chronic use of NSAIDs is less clear. In those who are untrained, it does not appear that regular NSAID use will impede growth in the short term, and at least one study indicates that it may in fact have a positive impact.

Given their reported impairment of satellite cell activity, however, longer-term NSAID use may well be detrimental, particularly in those who possess greater growth potential.


Fasted Resistance Training

This study (Deldicque L1, De Bock K, Maris M, Ramaekers M, Nielens H, Francaux M, Hespel P. Increased p70s6k phosphorylation during intake of a protein-carbohydrate drink following resistance exercise in the fasted state. Eur J Appl Physiol. 2010 Mar;108(4):791-800.) found that  subjects who lifted weights in a fasted state had a greater anabolic response to a postworkout meal). This was indicated by levels of p70S6 kinase, a muscle protein synthesis-­signaling mechanism that acts as an indicator of muscle growth, doubling in the fasted group compared with the fed group.



Strength Gains on Meat Protein vs Ovo-lacto-Vegetarian Protein Sources

Study of vegetarian diets vs meat as protein source diets and muscle gain in older men (Effects of an omnivorous diet compared with a lactoovovegetarian diet on resistance-training-induced changes in body composition and skeletal muscle in older men).

Conclusions: Consumption of a meat-containing diet contributed to greater gains in fat-free mass and skeletal muscle mass with RT in older men than did an LOV diet.

More details:


Maximal strength of the upper- and lower-body muscle groups that were exercised during RT increased by 10-38% (P < 0.001), independent of diet. The RT-induced changes in whole-body composition and skeletal muscle size differed significantly between the mixed- and LOV-diet groups (time-by-group interactions, P < 0. 05). With RT, whole-body density, fat-free mass, and whole-body muscle mass increased in the mixed diet group but decreased in the LOV- diet group. Type II muscle fiber area of the vastus lateralis muscle increased with RT for all men combined (P < 0.01), and the increase tended to be greater in the mixed-diet group (16.2 +/- 4.4 %) than in the LOV diet group (7.3 +/- 5.1%). Type I fiber area was unchanged with RT in both diet groups.

Another study showed favorable results for meat (Effect of protein source and quantity on protein metabolism in elderly women).

With the high-vegetable-protein diet, protein breakdown in the absorptive state was not inhibited to the same extent as during the high-animal-protein diet, resulting in less net protein synthesis during the high-vegetable-protein diet than during the high-animal-protein diet.