R E V I E W Open Access
How much protein can the body use in a
single meal for muscle-building?
Implications for daily protein distribution
Brad Jon Schoenfeld
and Alan Albert Aragon
Controversy exists about the maximum amount of protein that can be utilized for lean tissue-building purposes in a
single meal for those involved in regimented resistance training. It has been proposed that muscle protein synthesis is
maximized in young adults with an intake of ~ 20–25 g of a high-quality protein; anything above this amount is
believed to be oxidized for energy or transaminated to form urea and other organic acids. However, these findings are
specific to the provision of fast-digesting proteins without the addition of other macronutrients. Consumption of
slower-acting protein sources, particularly when consumed in combination with other macronutrients, would delay
absorption and thus conceivably enhance the utilization of the constituent amino acids. The purpose of this paper was
twofold: 1) to objectively review the literature in an effort to determine an upper anabolic threshold for per-meal
protein intake; 2) draw relevant conclusions based on the current data so as to elucidate guidelines for per-meal daily
protein distribution to optimize lean tissue accretion. Both acute and long-term studies on the topic were evaluated
and their findings placed into context with respect to per-meal utilization of protein and the associated implications to
distribution of protein feedings across the course of a day. The preponderance of data indicate that while consumption
of higher protein doses (> 20 g) results in greater AA oxidation, this is not the fate for all the additional ingested AAs as
some are utilized for tissue-building purposes. Based on the current evidence, we conclude that to maximize anabolism
one should consume protein at a target intake of 0.4 g/kg/meal across a minimum of four meals in order to reach a
minimum of 1.6 g/kg/day. Using the upper daily intake of 2.2 g/kg/day reported in the literature spread out over the
same four meals would necessitate a maximum of 0.55 g/kg/meal.
Keywords: Protein feeding pattern, Amino acid oxidation, Protein intake, Protein metabolism, Lean tissue mass
Controversy exists about the maximum amount of
protein that can be utilized for lean tissue-building pur-
poses in a single meal for those involved in regimented
resistance training. A long-held misperception in the lay
public is that there is a limit to how much protein can
be absorbed by the body. From a nutritional standpoint,
the term “absorption”describes the passage of nutrients
from the gut into systemic circulation. Based on this
definition, the amount of protein that can be absorbed is
virtually unlimited. Following digestion of a protein
source, the constituent amino acids (AA) are transported
through the enterocytes at the intestinal wall, enter the
hepatic portal circulation, and the AA that are not
utilized directly by the liver, then enter the bloodstream,
after which almost all the AA ingested become available
for use by tissues. While absorption is not a limiting
factor with respect to whole proteins, there may be
issues with consumption of individual free-form AA in
this regard. Specifically, evidence shows the potential for
competition at the intestinal wall, with AA that are
present in the highest concentrations absorbed at the
expense of those that are less concentrated .
It has been proposed that muscle protein synthesis
(MPS) is maximized in young adults with an intake
of ~ 20–25 g of a high-quality protein, consistent with
the “muscle full”concept; anything above this amount
is believed to be oxidized for energy or transaminated
* Correspondence: email@example.com
CUNY Lehman College, Department of Health Sciences, 250 Bedford Park
Blvd West, Bronx, NY 10468, USA
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Schoenfeld and Aragon Journal of the International Society of Sports Nutrition
to form alternative bodily compounds . The pur-
pose of this paper is twofold: 1) to objectively review
the literature in an effort to determine an upper ana-
bolic threshold for per-meal protein intake; 2) draw
relevant conclusions based on the current data so as
to elucidate guidelines for per-meal daily protein dis-
tribution to optimize lean tissue accretion.
Speed of digestion/absorption on muscle anabolism
In a study often cited as support for the hypothesis that
MPS is maximized at a protein dose of ~ 20–25 g, Areta
et al.  provided differing amounts of protein to
resistance-trained subjects over a 12-h recovery period
following performance of a multi-set, moderate repeti-
tion leg-extension exercise protocol. A total of 80 g of
whey protein was ingested in one of the following three
conditions: 8 servings of 10 g every 1.5 h; 4 servings of
20 g every 3 h; or 2 servings of 40 g every 6 h. Results
showed that MPS was greatest in those who consumed 4
servings of 20 g of protein, suggesting no additional
benefit, and actually a lower rise in MPS when consum-
ing the higher dosage (40 g) under the conditions
imposed in the study. These results extended similar
findings by Moore et al.  on whole-body nitrogen
Although the findings of Areta et al.  provide inter-
esting insight into the dose-related effects of protein
intake on muscle development, it is important to note
that a number of factors influence dietary protein me-
tabolism including the composition of the given protein
source, the composition of the meal, the amount of pro-
tein ingested, and the specifics of the exercise routine
. In addition, individual variables such as age, training
status, and the amount of lean body mass also impact
muscle-building outcomes. A major limitation in the
study by Areta et al.  is that total protein intake over
the 12-h study period was only 80 g, corresponding to
less than 1 g/kg of body mass. This is far below the
amount necessary to maximize muscle protein balance
in resistance-trained individuals who served as partici-
pants in the study [6,7]. Furthermore, the ecological
validity of this work is limited since habitual protein
intakes of individuals focused on muscle gain or reten-
tion habitually consume approximately 2–4 times this
amount per day [8,9].
It also should be noted that subjects in Areta et al. 
ingested nothing but whey protein throughout the post-
exercise period. Whey is a “fast-acting”protein; its
absorption rate has been estimated at ~ 10 g per hour
. At this rate, it would take just 2 h to fully absorb a
20-g dose of whey. While the rapid availability of AA
will tend to spike MPS, earlier research examining whole
body protein kinetics showed that concomitant oxida-
tion of some of the AA may result in a lower net protein
balance when compared to a protein source that is
absorbed at a slower rate . For example, cooked egg
protein has an absorption rate of ~ 3 g per hour ,
meaning complete absorption of an omelet containing
the same 20 g of protein would take approximately 7 h,
which may help attenuate oxidation of AA and thus pro-
mote greater whole-body net positive protein balance.
An important caveat is that these findings are specific to
whole body protein balance; the extent to which this re-
flects skeletal muscle protein balance remains unclear.
Although some studies have shown similar effects of
fast and slow proteins on net muscle protein balance
 and fractional synthetic rate [12–14], other studies
have demonstrated a greater anabolic effect of whey
compared to more slowly digested sources both at rest
[15,16], and after resistance exercise [16,17]. However,
the majority of these findings were during shorter testing
periods (4 h or less), whereas longer testing periods (5 h
or more) tend to show no differences between whey and
casein on MPS or nitrogen balance . Furthermore,
most studies showing greater anabolism with whey used
a relatively small dose of protein (≤20 g) [15–17]; it re-
mains unclear whether higher doses would result in
greater oxidation of fast vs slow-acting protein sources.
Compounding these equivocal findings, research exam-
ining the fate of intrinsically labeled whey and casein con-
sumed within milk found a greater incorporation of casein
into skeletal muscle . The latter finding should be
viewed with the caveat that although protein turnover in
the leg is assumed to be mostly reflective of skeletal
muscle, it is also possible that non-muscle tissues might
also contribute. Interestingly, the presence versus absence
of milk fat coingested with micellar casein did not delay
the rate of protein-derived circulating amino acid avail-
ability or myofibrillar protein synthesis . Furthermore,
the coingestion of carbohydrate with casein delayed diges-
tion and absorption, but still did not impact muscle pro-
tein accretion compared to a protein-only condition .
The implication is that accompanying macronutrients’
potential to alter digestion rates does not necessarily
translate to alterations in the anabolic effect of the protein
feeding –at least in the case of slow-digesting protein
such as casein. More fat and/or carbohydrate coingestion
comparisons need to be made with other proteins, subject
profiles, and relative proximity to training before drawing
Higher acute ‘anabolic ceiling’than previously thought?
More recently, Macnaughton et al.  employed a ran-
domized, double-blind, within-subject design whereby
resistance-trained men participated in two trials sepa-
rated by ~ 2 weeks. During one trial subjects received
20 g of whey protein immediately after performing a
total body resistance training bout; during the other trial
Schoenfeld and Aragon Journal of the International Society of Sports Nutrition (2018) 15:10 Page 2 of 6
the same protocol was instituted but subjects received a
40-g whey bolus following training. Results showed that
the myofibrillar fractional synthetic rate was ~ 20%
higher from consumption of the 40 g compared to the
20 g condition. The researchers speculated that the large
amount of muscle mass activated from the total body
RT bout necessitated a greater demand for AA that was
met by a higher exogenous protein consumption. It
should be noted that findings by McNaughton et al. 
are somewhat in contrast to previous work by Moore
et al. showing no statistically significant differences in
MPS between provision of a 20 g and 40 g dose of whey
in young men following a leg extension bout, although
the higher dose produced an 11% greater absolute
increase . Whether differences between intakes
higher than ~ 20 g per feeding are practically meaningful
remain speculative, and likely depend on the goals of the
Given that muscular development is a function of the
dynamic balance between MPS and muscle protein
breakdown (MPB), both of these variables must be
considered in any discussion on dietary protein dosage.
Kim et al.  endeavored to investigate this topic by
provision of either 40 or 70 g of beef protein consumed
as part of a mixed meal on two distinct occasions sepa-
rated by a ~ 1 week washout period. Results showed that
the higher protein intake promoted a significantly
greater whole-body anabolic response, which was pri-
marily attributed to a greater attenuation of protein
breakdown. Given that participants ate large, mixed
meals as whole foods containing not only protein, but
carbohydrates and dietary fats as well, it is logical to
speculate that this delayed digestion and absorption of
AAs compared to liquid consumption of isolated protein
sources. This, in turn, would have caused a slower
release of AA into circulation and hence may have con-
tributed to dose-dependent differences in the anabolic
response to protein intake. A notable limitation of the
study is that measures of protein balance were taken at
the whole-body level and thus not muscle-specific. It
therefore can be speculated that some if not much of
anti-catabolic benefits associated with higher protein in-
take was from tissues other than muscle, likely the gut.
Even so, protein turnover in the gut potentially provides
an avenue whereby accumulated amino acids can be re-
leased into the systemic circulation to be used for MPS,
conceivably enhancing anabolic potential . This
hypothesis remains speculative and warrants further in-
vestigation. It would be tempting to attribute these
marked reductions in proteolysis to higher insulin re-
sponses considering the inclusion of a generous amount
of carbohydrate in the meals consumed. Although insu-
lin is often considered an anabolic hormone, its primary
role in muscle protein balance is related to anti-catabolic
effects . However, in the presence of elevated plasma
AAs, the effect of insulin elevations on net muscle
protein balance plateaus within a modest range of 15–
30 mU/L [27,28]. Given evidence that a 45 g dose of
whey protein causes insulin to rise to levels sufficient to
maximize net muscle protein balance , it would
seem that the additional macronutrients consumed in
the study by Kim et al.  had little bearing on results.
Although the previously discussed studies offer insight
into how much protein the body can utilize in a given
feeding, acute anabolic responses are not necessarily as-
sociated with long-term muscular gains . The topic
can only be answered by assessing the results of longitu-
dinal studies that directly measure changes in lean mass
with provision of varying protein dosages, as well as pro-
teins of varying speeds of digestion/absorption.
Wilborn et al. , found no difference in lean mass
gains after 8 weeks of pre- and post-resistance exercise
supplementation with either whey or casein. Similarly, a
lack of between-group differences in lean mass gain was
found by Fabre et al.  when comparing the following
whey/casein protein ratios consumed postexercise: 100/
0, 50/50, 20/80.
In a 14-day study of elderly women, Arnal et al. 
demonstrated that providing a majority of daily protein
(79%) in a single meal (pulse pattern) resulted in a
greater retention of fat-free mass compared to an evenly
distributed intake partitioned over four daily meals
(spread pattern). A follow-up study by the same lab in
young women reported similar effects of pulse versus
spread patterns of protein intake . The combined
findings of these studies indicate that muscle mass is
not negatively affected by consuming the majority of
daily protein as a large bolus. However, neither study
employed regimented resistance training thereby lim-
iting generalizability to individuals involved in intense
Insights into the effects of protein dosage can also be
gleaned from studies on intermittent fasting (IF). Typical
IF protocols require intake of daily nutrients, including
protein, in a narrow time-frame –usually less than 8 h
–followed by a prolonged fast. A recent systematic re-
view concluded that IF has similar effects on fat-free
mass compared with continuous eating protocols .
However, the studies reviewed in the analysis generally
involved suboptimal protein intakes consumed as part of
a low-energy diet without a resistance training compo-
nent, again limiting the ability to extrapolate findings to
Helping to fill this literature gap is an 8-week trial by
Tinsley et al. , comparing a time-restricted feeding
(TRF) protocol of 20-h fasting/4-h feeding cycles done
Schoenfeld and Aragon Journal of the International Society of Sports Nutrition (2018) 15:10 Page 3 of 6
4 days per week, with a normal-diet group (ND) in un-
trained subjects doing resistance training 3 days per week.
The TRF group lost body weight via lower energy intake
(667 kcal less on fasting vs. non-fasting days), but did not
significantly lose lean mass (0.2 kg); ND gained lean mass
(2.3 kg), but not to a statistically significant degree, al-
though the magnitude of differences raises the possibility
that these findings may be practically meaningful. Perhaps
most interestingly, biceps brachii and rectus femoris cross
sectional area showed similar increases in both groups
despite the 20-h fasting cycles and concentrated feeding
cycles in TRF, suggesting that the utilization of protein
intake in the ad libitum 4-h feeding cycles was not ham-
pered by an acute ceiling of anabolism. Unfortunately,
protein and enrgy were not equated in this study. Subse-
quently, an 8-week trial by Moro et al. using
resistance-trained subjects on a 16-h fasting/8-h TRF cycle
found significantly greater fat loss in TRF vs. ND (1.62 vs.
0.31 kg) while lean mass remained unchanged in both
groups. These findings further call into question the con-
cern for breaching a certain threshold of protein intake
In contrast to the above findings showing neutral-to-
positive effects of a temporally concentrated meal intake,
Arciero et al.  compared 3 diets: 2 high-protein (35%
of total energy) diets consisting of 3 (HP3) and 6 meals/
day (HP6), and a traditional protein intake (15% of total
energy) consumed in 3 meals/day (TD3). During the ini-
tial 28-day eucaloric phase, HP3 and HP6 consumed
protein at 2.27 & 2.15 g/kg, respectively, while TD3 con-
sumed 0.9 g/kg. HP6 was the only goup that significantly
gained lean mass. During the subsequent 28-day eucalo-
ric phase, HP3 and HP6 consumed protein at 1.71 &
1.65 g/kg, respectively, while TD3 consumed 0.75 g/kg.
HP6 maintained its lean mass gain, outperforming the
other 2 treatments in this respect (HP actually showed a
significant loss of lean mass compared to the control).
The discrepancy between the latter findings and those in
the IF/TRF trials remains to be reconciled. In any case,
it is notable that comparisons in this vein specifically
geared toward the goal of muscle gain, hypercaloric
comparisons in particular, are lacking.
An important distinction needs to be made between
acute meal challenges comparing different protein
amounts (including serial feedings in the acute phase
following resistance training) and chronic meal feedings
comparing different protein distributions through the
day, over the course of several weeks or months. Longi-
tudinal studies examining body composition have not
consistently corroborated the results of acute studies
examining muscle protein flux. Quantifying a maximum
amount of protein per meal that can be utilized for
muscle anabolism has been a challenging pursuit due to
the multitude of variables open for investigation. Per-
haps the most comprehensive synthesis of findings in
this area has been done by Morton et al. , who con-
cluded that 0.4 g/kg/meal would optimally stimulate
MPS. This was based on the addition of two standard
deviations to their finding that 0.25 g/kg/meal maximally
stimulates MPS in young men. In line with this hypoth-
esis, Moore et al.  mentioned the caveat that their
findings were estimated means for maximizing MPS, and
that the dosing ceilings can be as high as ~ 0.60 g/kg for
some older men and ~ 0.40 g/kg for some younger men.
Importantly, these estimates are based on the sole
provision of a rapidly digesting protein source that would
conceivably increase potential for oxidation of AA when
consumed in larger boluses. It seems logical that a slower-
acting protein source, particularly when consumed in
combination with other macronutrients, would delay
absorption and thus enhance the utilization of the con-
stituent AA. However, the practical implications of this
phenomenon remain speculative and questionable .
The collective body of evidence indicates that total daily
protein intake for the goal of maximizing resistance
training-induced gains in muscle mass and strength is ap-
proximately 1.6 g/kg, at least in non-dieting (eucaloric or
hypercaloric) conditions . However, 1.6 g/kg/day should
not be viewed as an ironclad or universal limit beyond
which protein intake will be either wasted or used for
physiological demands aside from muscle growth. A re-
cent meta-analysis on protein supplementation involving
resistance trainees reported an upper 95% confidence
interval (CI) of 2.2 g/kg/day . Bandegan et al. also
showed an upper CI of 2.2 g/kg/day in a cohort of young
male bodybuilders, although the method of assessment
(indicator amino acid oxidation technique) used in this
study has not received universal acceptance for determin-
ing optimal protein requirements. This reinforces the
practical need to individualize dietary programming, and
remain open to exceeding estimated averages. It is there-
fore a relatively simple and elegant solution to consume
protein at a target intake of 0.4 g/kg/meal across a
minimum of four meals in order to reach a minimum of
1.6 g/kg/day –if indeed the primary goal is to build
muscle. Using the upper CI daily intake of 2.2 g/kg/day
over the same four meals would necessitate a maximum
of 0.55 g/kg/meal. This tactic would apply what is cur-
rently known to maximize acute anabolic responses as
well as chronic anabolic adaptations. While research
shows that consumption of higher protein doses (> 20 g)
results in greater AA oxidation , evidence indicates
that this is not the fate for all the additional ingested AAs
as some are utilized for tissue-building purposes. Further
research is nevertheless needed to quantify a specific
upper threshold for per-meal protein intake.
Schoenfeld and Aragon Journal of the International Society of Sports Nutrition (2018) 15:10 Page 4 of 6
Availability of data and materials
Brad Schoenfeld conceived of the article. Both authors equally contributed
to the writing of the manuscript. Both authors read and approved the final
Ethics approval and consent to participate
Consent for publication
Brad Schoenfeld serves on the scientific advisory board for Dymatize
Nutrition. The authors declare no other conflicts of interest.
Springer Nature remains neutral with regard to jurisdictional claims in
published maps and institutional affiliations.
CUNY Lehman College, Department of Health Sciences, 250 Bedford Park
Blvd West, Bronx, NY 10468, USA.
California State University, 18111 Nordhoff
St, Northridge, CA 91330, USA.
Received: 19 September 2017 Accepted: 20 February 2018
1. Gropper SS, Smith JL, Groff JL:Advanced Nutrition and Human Metabolism.
Belmont, CA: Wadsworth Cengage Learning; 2009.
2. Morton RW, McGlory C, Phillips SM. Nutritional interventions to augment
resistance training-induced skeletal muscle hypertrophy. Front Physiol. 2015;
3. Areta JL, Burke LM, Ross ML, Camera DM, West DW, Broad EM, Jeacocke NA,
Moore DR, Stellingwerff T, Phillips SM, Hawley JA, Coffey VG. Timing and
distribution of protein ingestion during prolonged recovery from resistance
exercise alters myofibrillar protein synthesis. J Physiol. 2013;591(Pt 9):2319–31.
4. Moore DR, Areta J, Coffey VG, Stellingwerff T, Phillips SM, Burke LM, Cleroux
M, Godin JP, Hawley JA. Daytime pattern of post-exercise protein intake
affects whole-body protein turnover in resistance-trained males. Nutr Metab
(Lond). 2012;9(1):91. -7075-9-91
5. Bilsborough S, Mann N. A review of issues of dietary protein intake in
humans. Int J Sport Nutr Exerc Metab. 2006;16(2):129–52.
6. Morton RW, Murphy KT, McKellar SR, Schoenfeld BJ, Henselmans M, Helms
E, Aragon AA, Devries MC, Banfield L, Krieger JW, Phillips SM. A systematic
review, meta-analysis and meta-regression of the effect of protein
supplementation on resistance training-induced gains in muscle mass and
strength in healthy adults. Br J Sports Med. 2017;
7. Bandegan A, Courtney-Martin G, Rafii M, Pencharz PB, Lemon PW. Indicator
amino acid-derived estimate of dietary protein requirement for male
bodybuilders on a nontraining day is several-fold greater than the current
recommended dietary allowance. J Nutr. 2017;147(5):850–7.
8. Spendlove J, Mitchell L, Gifford J, Hackett D, Slater G, Cobley S, O'Connor H.
Dietary intake of competitive bodybuilders. Sports Med. 2015;45(7):1041–63.
9. Antonio J, Ellerbroek A, Silver T, Vargas L, Peacock C: The effects of a high
protein diet on indices of health and body composition–a crossover trial in
resistance-trained men.J Int Soc Sports Nutr 2016, 13:3–016–0114-2.
10. Dangin M, Boirie Y, Guillet C, Beaufrere B: Influence of the protein digestion
rate on protein turnover in young and elderly subjects.J Nutr 2002, 132(10):
11. Tipton KD, Elliott TA, Cree MG, Wolf SE, Sanford AP, Wolfe RR. Ingestion of
casein and whey proteins result in muscle anabolism after resistance
exercise. Med Sci Sports Exerc. 2004;36(12):2073–81.
12. Mitchell CJ, McGregor RA, D'Souza RF, Thorstensen EB, Markworth JF,
Fanning AC, Poppitt SD, Cameron-Smith D. Consumption of milk protein or
whey protein results in a similar increase in muscle protein synthesis in
middle aged men. Nutrients. 2015;7(10):8685–99.
13. Reitelseder S, Agergaard J, Doessing S, Helmark IC, Lund P, Kristensen NB,
Frystyk J, Flyvbjerg A, Schjerling P, van Hall G, Kjaer M, Holm L. Whey and
casein labeled with L-[1-13C]leucine and muscle protein synthesis: effect of
resistance exercise and protein ingestion. Am J Physiol Endocrinol Metab.
14. Dideriksen KJ, Reitelseder S, Petersen SG, Hjort M, Helmark IC, Kjaer M, Holm
L. Stimulation of muscle protein synthesis by whey and caseinate ingestion
after resistance exercise in elderly individuals. Scand J Med Sci Sports. 2011;
15. Pennings B, Boirie Y, Senden JM, Gijsen AP, Kuipers H, van Loon LJ. Whey
protein stimulates postprandial muscle protein accretion more effectively
than do casein and casein hydrolysate in older men. Am J Clin Nutr. 2011;
16. Burd NA, Yang Y, Moore DR, Tang JE, Tarnopolsky MA, Phillips SM. Greater
stimulation of myofibrillar protein synthesis with ingestion of whey protein
isolate v. Micellar casein at rest and after resistance exercise in elderly men.
Br J Nutr. 2012;108(6):958–62.
17. Tang JE, Moore DR, Kujbida GW, Tarnopolsky MA, Phillips SM. Ingestion of
whey hydrolysate, casein, or soy protein isolate: effects on mixed muscle
protein synthesis at rest and following resistance exercise in young men.
J Appl Physiol (1985). 2009;107(3):987–92.
18. Witard OC, Wardle SL, Macnaughton LS, Hodgson AB, Tipton KD. Protein
considerations for Optimising skeletal muscle mass in healthy young and
older adults. Nutrients. 2016;8(4):181.
19. Soop M, Nehra V, Henderson GC, Boirie Y, Ford GC, Nair KS. Coingestion of
whey protein and casein in a mixed meal: demonstration of a more
sustained anabolic effect of casein. Am J Physiol Endocrinol Metab. 2012;
20. Gorissen SHM, Burd NA, Kramer IF, van Kranenburg J, Gijsen AP, Rooyackers O,
van Loon LJC. Co-ingesting milk fat with micellar casein does not affect
postprandial protein handling in healthy older men. Clin Nutr. 2017;36(2):429–37.
21. Gorissen SH, Burd NA, Hamer HM, Gijsen AP, Groen BB, van Loon LJ.
Carbohydrate coingestion delays dietary protein digestion and absorption
but does not modulate postprandial muscle protein accretion. J Clin
Endocrinol Metab. 2014;99(6):2250–8.
22. Macnaughton LS, Wardle SL, Witard OC, McGlory C, Hamilton DL, Jeromson
S, Lawrence CE, Wallis GA, Tipton KD. The response of muscle protein
synthesis following whole-body resistance exercise is greater following 40 g
than 20 g of ingested whey protein. Physiol Rep. 2016;4(15) https://doi.org/
23. Moore DR, Robinson MJ, Fry JL, Tang JE, Glover EI, Wilkinson SB, Prior T,
Tarnopolsky MA, Phillips SM. Ingested protein dose response of muscle and
albumin protein synthesis after resistance exercise in young men. Am J Clin
24. Kim IY, Schutzler S, Schrader A, Spencer HJ, Azhar G, Ferrando AA, Wolfe RR.
The anabolic response to a meal containing different amounts of protein is
not limited by the maximal stimulation of protein synthesis in healthy
young adults. Am J Physiol Endocrinol Metab. 2016;310(1):E73–80.
25. Deutz NE, Wolfe RR. Is there a maximal anabolic response to protein intake
with a meal? Clin Nutr. 2013;32(2):309–13.
26. Abdulla H, Smith K, Atherton PJ, Idris I. Role of insulin in the regulation of
human skeletal muscle protein synthesis and breakdown: a systematic
review and meta-analysis. Diabetologia. 2016;59(1):44–55.
27. Greenhaff PL, Karagounis LG, Peirce N, Simpson EJ, Hazell M, Layfield R,
Wackerhage H, Smith K, Atherton P, Selby A, Rennie MJ. Disassociation
between the effects of amino acids and insulin on signaling, ubiquitin
ligases, and protein turnover in human muscle. Am J Physiol Endocrinol
28. Rennie MJ, Bohe J, Smith K, Wackerhage H, Greenhaff P. Branched-chain
amino acids as fuels and anabolic signals in human muscle. J Nutr. 2006;
29. Power O, Hallihan A, Jakeman P. Human insulinotropic response to oral
ingestion of native and hydrolysed whey protein. Amino Acids. 2009;37(2):
Schoenfeld and Aragon Journal of the International Society of Sports Nutrition (2018) 15:10 Page 5 of 6
30. Mitchell CJ, Churchward-Venne TA, Parise G, Bellamy L, Baker SK, Smith K,
Atherton PJ, Phillips SM. Acute post-exercise myofibrillar protein synthesis is
not correlated with resistance training-induced muscle hypertrophy in
young men. PLoS One. 2014;9(2):e89431.
31. Wilborn CD, Taylor LW, Outlaw J, Williams L, Campbell B, Foster CA, Smith-
Ryan A, Urbina S, Hayward S. The effects of pre- and post-exercise whey vs.
casein protein consumption on body composition and performance
measures in collegiate female athletes. J Sports Sci Med. 2013;12(1):74–9.
32. Fabre M, Hausswirth C, Tiollier E, Molle O, Louis J, Durguerian A, Neveux N,
Bigard X. Effects of Postexercise protein intake on muscle mass and
strength during resistance training: is there an optimal ratio between fast
and slow proteins? Int J Sport Nutr Exerc Metab. 2017;27(5):448–57.
33. Arnal MA, Mosoni L, Boirie Y, Houlier ML, Morin L, Verdier E, Ritz P, Antoine
JM, Prugnaud J, Beaufrere B, Mirand PP. Protein pulse feeding improves
protein retention in elderly women. Am J Clin Nutr. 1999;69(6):1202–8.
34. Arnal MA, Mosoni L, Boirie Y, Houlier ML, Morin L, Verdier E, Ritz P, Antoine
JM, Prugnaud J, Beaufrere B, Mirand PP. Protein feeding pattern does not
affect protein retention in young women. J Nutr. 2000;130(7):1700–4.
35. Seimon RV, Roekenes JA, Zibellini J, Zhu B, Gibson AA, Hills AP, Wood RE,
King NA, Byrne NM, Sainsbury A. Do intermittent diets provide physiological
benefits over continuous diets for weight loss? A systematic review of
clinical trials. Mol Cell Endocrinol. 2015;418(Pt 2):153–72.
36. Tinsley GM, Forsse JS, Butler NK, Paoli A, Bane AA, La Bounty PM, Morgan GB,
Grandjean PW. Time-restricted feeding in young men performing resistance
training: a randomized controlled trial. Eur J Sport Sci. 2017;17(2):200–7.
37. Moro T, Tinsley G, Bianco A, Marcolin G, Pacelli QF, Battaglia G, Palma A, Gentil P,
Neri M, Paoli A. Effects of eight weeks of time-restricted feeding (16/8) on basal
metabolism, maximal strength, body composition, inflammation, and
cardiovascular risk factors in resistance-trained males. J Transl Med. 2016;14(1):290.
38. Arciero PJ, Ormsbee MJ, Gentile CL, Nindl BC, Brestoff JR, Ruby M. Increased
protein intake and meal frequency reduces abdominal fat during energy
balance and energy deficit. Obesity (Silver Spring). 2013;21(7):1357–66.
39. Moore DR, Churchward-Venne TA, Witard O, Breen L, Burd NA, Tipton KD,
Phillips SM. Protein ingestion to stimulate myofibrillar protein synthesis
requires greater relative protein intakes in healthy older versus younger
men. J Gerontol A Biol Sci Med Sci. 2015;70(1):57–62.
40. Witard OC, Jackman SR, Breen L, Smith K, Selby A, Tipton KD. Myofibrillar
muscle protein synthesis rates subsequent to a meal in response to
increasing doses of whey protein at rest and after resistance exercise.
Am J Clin Nutr. 2014;99(1):86–95.
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