Timeline of proteins

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This is a timeline of proteins, a class of macromolecules in the form of polymer chains made of amino acids. Proteins are essential nutrients for the human body. This timeline focuses on proteins from a nutritional perspective.

Sample questions

The following are some interesting questions that can be answered by reading this timeline:

  • What are some notable publications specialized in proteins?
    • Sort the full timeline by "Event type" and look for the group of rows with value "Literature".

Big picture

Time period Development summary More details
1920–1950 "From 1920 to 1950 nutritional research centered on the discovery of individual vita mins and amino acids, and there was little interest in human protein requirements, or in the possibility of their not being met."[1]
1950s–1960s "In the 1950s and 1960s protein again received priority attention. The "World Protein Gap" was considered the major cause of infant mortality and retarded development in the Third World but a problem that could be solved by the application of sophisticated technology."[1]

Numerical and visual data

The table below shows daily protein intake (g) by age, education, work, status, income and geographical region, in Chinese women from 1991 to 2015.

1991 Mean 1991 SE 1993 Mean 1993 SE 1997 Mean 1997 SE 2000 Mean 2000 SE 2004 Mean 2004 SE 2006 Mean 2006 SE 2009 Mean 2009 SE 2011 Mean 2011 SE 2015 Mean 2015 SE
Age group (year):
18-49 70.3 0.4 69.9 0.4 67.9 0.4 65.7 0.4 65.0 0.4 65.2 0.4 63.9 0.4 61.0 0.4 57.7 0.4
50-64 67.7 0.7 66.3 0.9 63.6 0.8 63.9 0.7 64.8 0.7 64.6 0.6 62.4 0.6 59.0 0.5 56.2 0.4
Education level:
Primary/ illiterate 69.6 0.5 68.9 0.5 66.0 0.5 63.7 0.5 64.1 0.5 64.5 0.5 62.7 0.5 58.0 0.5 57.0 0.5
Middle school 69.9 0.6 69.8 0.7 67.9 0.6 66.3 0.6 64.2 0.6 65.6 0.6 63.9 0.5 60.8 0.5 58.2 0.6
High/above 70.4 0.8 69.9 0.9 68.7 0.8 67.0 0.7 67.3 0.7 64.9 0.7 63.8 0.7 62.2 0.6 56.3 0.4
Low 68.9 0.6 68.7 0.6 65.7 0.6 64.0 0.6 62.7 0.6 64.9 0.6 63.0 0.5 59.8 0.5 55.7 0.5
Medium 70.0 0.6 69.1 0.6 67.7 0.6 64.9 0.6 66.2 0.6 65.2 0.6 63.1 0.6 59.4 0.5 55.9 0.5
High 70.5 0.6 70.3 0.6 67.7 0.6 67.0 0.6 65.9 0.6 65.0 0.6 64.1 0.5 61.5 0.5 59.2 0.5
Rural 69.6 0.5 70.4 0.6 69.7 0.6 67.8 0.6 66.8 0.6 66.6 0.7 64.0 0.6 61.3 0.5 55.4 0.3
Urban 69.9 0.4 68.8 0.4 65.8 0.4 64.1 0.4 64.1 0.4 64.3 0.4 63.2 0.4 59.7 0.3 59.5 0.4
BMI category:
Underweight 64.9 1.1 67.3 1.2 63.8 1.2 63.5 1.4 63.9 1.5 62.5 1.4 59.2 1.1 59.0 1.2 56.3 1.0
Normal 69.9 0.4 68.9 0.4 66.9 0.4 65.5 0.4 64.6 0.5 64.7 0.4 63.6 0.4 60.6 0.4 57.0 0.4
Overweight/ obesity 71.5 0.7 71.3 0.7 68.3 0.7 65.2 0.6 65.8 0.6 66.1 0.6 63.9 0.5 60.0 0.5 57.2 0.4
Total 69.8 0.3 69.3 0.4 67.1 0.3 65.3 0.3 64.9 0.4 65.0 0.3 63.4 0.3 60.3 0.3 57.0 0.3

The table below shows changing views of the role of amino acids in human nutrition.

1954 Indispensable 1994 Indispensable 1994 Conditionally indispensable 1954 Dispensable 1994 Dispensable
Valine Valine Glycine Glycine Glutamic acid
Isoleucine Isoleucine Cystine Cystine Alanine
Leucine Leucine Glutamine Glutamic acid Serine
Lysine Lysine Tyrosine Tyrosine Aspartic acid
Methionine Methionine Proline Proline Asparagine
Phenylalanine Phenylalanine Arginine Arginine
Threonine Threonine Taurine Alanine
Tryptophan Tryptophan Serine
Histidine Aspartic acid

The table below shows estimates made at different times of the protein and energy requirements of children at 1 year of age.[1]

Year Protein Energy Protein energy Source
g/kg body wt kcal/kg body wt  % of total energy
1948 3.3 100 13.2 USA
1957 2.0 100 8.0 FAO
1964 2.5 100 10.0 USA
1965 1.1 100 4.4 FAO/WHO
1968 1.8 100 7.2 USA
1969 1.3 110 4.7 UK
1973 1.27 105 4.8 FAO/WHO
1974 1.35 100 5.4 USA

Google Schoolar

The following table summarizes per-year mentions on Google Scholar as of October 3, 2021.

Year "protein"
1900 405
1910 925
1920 1,910
1930 3,360
1940 5,070
1950 9,590
1960 21,100
1970 64,500
1980 170,000
1990 472,000
2000 1,110,000
2010 1,600,000
2020 274,000
Protein gsch.png

The table below shows dietary requirements of protein (g per kg body weight per day).[2]

Group Age (Years) IOM 2005 FAO/ WHO/ UNU 1985 FAO/ WHO/ UNU 2007
Infants 0.3-0.5 1.52 1.75 1.31
0.75-1.0 1.50 1.57 1.14
Children 1-3 1.10 1.18 1.02
4-8 0.95 1.05 0.92
Adolescents 9-13 0.95 0.99 0.90
14-18 (boys) 0.85 0.97 0.87
14-18 (girl) 0.85 0.94 0.85
Adults >19 0.80 0.75 0.83

The table below shows dietary requirements of EAA by healthy human adults.

EAA Estimates from N balance experiments Men Estimates from N balance experiments Women MIT values (tracer studies) (2000) IOM (2005) FAO/ WHO UNU (2007)
His - - - 14 10
Ile 10 9.17 23 19 20
Leu 15.7 12.1 40 42 39
Lys 11.4 9.07 30 38 30
Met 2.36 3.23 - - -
Met+Cys 15.7 11.7 13 19 15
Phe 4.29 4.30 - - -
Phe+Tyr 15.7 - 39 33 25
Thr 7.14 6.25 15 20 15
Trp 3.57 2.80 6 5 4
Val 11.4 10.4 20 24 26
Total 90.6 65.8 186 214 184


Google Trends

The comparative chart below shows Google Trends data for Protein (Nutrient) and Protein (Topic) from January 2004 to October 2021, when the screenshot was taken. Interest is also ranked by country and displayed on world map.[3]

Protein gt.png

Google Ngram Viewer

The comparative chart below shows Google Ngram Viewer data for Protein, amino acid and calorie from 1800 to 2019.[4]

Protein ngram.png

Wikipedia Views

The chart below shows pageviews of the English Wikipedia article Protein, from July 2015 to September 2021.[5]

Protein wv.png

Full timeline

Year Event type Details Component functions/benefits (when applicable) Food source (when applicable)
1806 Scientific development Asparagine is first isolated in a crystalline form by French chemists Louis Nicolas Vauquelin and Pierre Jean Robiquet (then a young assistant) from asparagus juice.[6][7] A non-essential amino acid in humans[8], it is closely related to aspartic acid.[9] "According to the research, L-asparagine is able to protect cancer cells from dying due to a loss of glutamine."[10] Rich food sources include dairy, whey, beef, poultry, eggs, fish, seafood, asparagus, potatoes, legumes, nuts, seeds, soy, and whole grains. Poor food sources include most fruits and vegetables.[11]
1810 Scientific development English chemist William Hyde Wollaston indirectly discovers cystine, when managing to isolate a crystalline substance from urinary calculi (kidney stones) and calls it “cystic oxide”.[12] Cystine is the oxidized dimer form of the amino acid cysteine Cystine is a non-essential amino acid important for making protein, and for other metabolic functions.[13]
1816 Scientific development French physiologist François Magendie demonstrates that dogs would die if fed nothing but carbohydrates or fat, i.e., the principal nonnitrogenous food components.[1]
1819 Scientific development The discovery of leucine is attributed to French chemist Joseph Proust who reports its separation from fermented milk curds.[14] Leucine is one of the three branched-chain amino acids (BCAA), along with isoleucine and valine.[15] Like valine, leucine is critical for protein synthesis and muscle repair.[16] Rich food sources include chicken, beef, pork, fish (tuna), tofu, canned beans, milk, cheese, squash seeds, and eggs.[17]
1820 Scientific development Glycine is discovered by French chemist Henri Braconnot when he hydrolyzes gelatin by boiling it with sulfuric acid.[18] Glycine is the main amino acid in collagen, the most abundant protein in the body. It is a simple amino acid with no L or D chemical configuration.[19] Glycine is structural of connective tissue, such as bone, skin, ligaments, tendons and cartilage.[20][21] It is found in high-protein foods including meat, fish, eggs, dairy and legumes.[22]
1827 Scientific development Aspartic acid (or aspartate) is first discovered by Auguste-Arthur Plisson and Étienne Ossian Henry.[23] It is a non-essential amino acid, meaning that it is readily and naturally synthesized by mammals.[24] D-aspartic acid (D-AA) regulates testosterone synthesis and may act on a stimulatory receptor (NMDA).[25]
1827 Scientific development Taurine is first isolated from ox bile by German scientists Friedrich Tiedemann and Leopold Gmelin.[26] It is a type of chemical called an amino sulfonic acid. It occurs naturally in the human body.[27] Taurine is found naturally in meat, fish, dairy products and human milk, and it's also available as a dietary supplement.[28]
1833 Scientific development The empirical formula for asparagine is first determined by French chemists Antoine François Boutron Charlard and Théophile-Jules Pelouze. In the same year, German chemist Justus Liebig provides a more accurate formula.[29][30]
1846 Scientific development English industrial chemist Edmund Ronalds discovers taurine in human bile.[31]
1846 Scientific development Tyrosine is first discovered by German chemist Justus von Liebig in the protein casein from cheese.[32][33] It is one of the 20 standard amino acids that are used by cells to synthesize proteins.[34] Tyrosine is an essential amino acid, and an aromatic amino acid derived from phenylalanine by hydroxylation in the para position.[35] Tyrosine is a popular dietary supplement used to improve alertness, attention and focus.[34] "Tyrosine is found in soy products, chicken, turkey, fish, peanuts, almonds, avocados, bananas, milk, cheese, yogurt, cottage cheese, lima beans, pumpkin seeds, and sesame seeds."[36]
1858 Scientific development French chemist Auguste Cahours determines that glycine is an amine of acetic acid.[37]
1859 Scientific development German scientists Nikolaus Friedreich and Friedrich August Kekulé von Stradonitz demonstrate that, rather than consisting of cellulose, "amyloid" actually is rich in protein.[38] "Amyloid is an aggregated protein structure consisting of unbranched microscopic fibrils often found in dense tissue deposits and associated with a variety of human diseases, including a number of significant neurodegenerative disorders."[39]
1865 Scientific development Serine is first obtained by Emil Cramer from silk protein, a particularly rich source. Its name is derived from the Latin for silk, sericum.[40] Serine comes in two forms: L-serine and D-serine.[41] "D-serine is used for schizophrenia, Parkinson disease, and memory and thinking skills (cognitive function), and many other conditions."[42] Serine is found in soybeans, nuts (especially peanuts, almonds, and walnuts), eggs, chickpeas, lentils, meat, and fish (especially shellfish).[43]
1866 Scientific development Glutamic acid is discovered and identified by German chemist Karl Heinrich Ritthausen.[44] Glutamic acid is a non-essential amino acid that occurs in plants and animals and is formed via protein metabolism.[45]
1869 Scientific development "The famous experiment of the physiolo gists Fick and Wislicenus in 1869 (10), in which they measured their urinary nitrogen during and after climbing a Swiss mountain, seemed to demonstrate conclusively that there was no apparent extra breakdown of protein that would be required to provide the energy used in the climb"[1]
1879 Scientific development German chemist Ernst Schulze and Johann Barbieri first identify phenylalanine as a constituent of plant proteins.[46][47][48] Phenylalanine is one of the nine essential amino acids. It occurs naturally in many protein-rich foods, such as milk, eggs and meat.[49]
1882 Scientific development German chemists Emil Erlenmeyer and Andreas Lipp first synthesize phenylalanine from phenylacetaldehyde, hydrogen cyanide, and ammonia.[50]
1883 Scientific development "German chemists Ernst. Schulze and E. Bosshard isolated L-glutamine from the juice of sugarbeets. It is the most common amino acid in human blood and a key component of proteins."[51] The most abundant free amino acid in the body, glutamine is produced in the muscles and is distributed by the blood to the organs that need it.[52]
1886 Scientific development "Schulze was also the first to isolate L-arginine, in this case from lupin seedlings. It is also an important amino acid in protein biosynthesis."[51]
1889 Scientific development Lysine is first isolated by German biological chemist Ferdinand Heinrich Edmund Drechsel from the protein casein in milk.[53] It is an essential amino acid. Lysine is important for normal growth and muscle turnover and used to form carnitine, a substance found in most cells of the body.[54]
1896 Scientific development Histidine is first isolated by German physician Albrecht Kossel and Sven Gustaf Hedin.[55] Histidine is a semi-essential amino acid (children should obtain it from food).[56] Histidine is needed in humans for growth and tissue repair.[57] It is important for maintenance of myelin sheaths that protect nerve cells and is metabolized to the neurotransmitter histamine.[57] Histidine is abundant in meat, fish, poultry, nuts, seeds, and whole grains.[58]
1899 Scientific development Cystine is isolated from the horn of a cow.[59]
1890s Scientific development The United States Department of Agriculture recommends over 110 g dietary protein per day for working men.[1]
1900 Recommendation The official United States Department of Agriculture recommendations around this time are concerned only with providing sufficient protein and energy and how these could be purchased economically.[1]
1900 Scientific development German chemist Richard Willstätter first isolates proline[60] and publishes the synthesis of proline from phthalimide propylmalonic ester.[61] A nonessential amino acid[62], proline is helpful for repairing damage to the skin.[63]
1901 Scientific development German chemist Hermann Emil Fischer first isolates Valine from casein.[64] A branched-chain essential amino acid with stimulant activity, valine promotes muscle growth and tissue repair. It is a precursor in the penicillin biosynthetic pathway.[65] Valine is found mainly in protein food sources such as meats, fish, soy, and dairy.[66]
1901 Scientific development British biochemists Frederick Gowland Hopkins and Sydney William Cole discover tryptophan in the milk derivative casein.[67] An essencial amino acid, tryptophan is vital for a wide variety of metabolic functions that affect the mood, cognition, and behavior.[68]
1902 Scientific development The structure of serine is established.[69]
1902 Scientific development German chemists Emil Fischer and Fritz Weigert determine lysine's chemical structure by synthesizing it.[70]
1902 Scientific development Emil Fischer isolates hydroxyproline from hydrolyzed gelatin.[71]
1902 Recommendation W. O. Atwater recommends a dietary intake of 125 g protein per day for the average American adult, because he thinks that U.S. workmen generally work harder than Germans.W. O. Atwater, Principles of Nutrition and Nutritive Value of Food, USDA Farmers’ Bull, no. 142, 1902
1903 Scientific development German chemist Felix Ehrlich discovers isoleucine in hemoglobin.[72] Isoleucine is an amino acid present in most common proteins.[73] It is an essential amino acid.[74] Isoleucine is critical in physiological functions of the whole body, such as growth, immunity, protein metabolism, fatty acid metabolism and glucose transportation. It can improve the immune system, including immune organs, cells and reactive substances.[75] Isoleucine is abundant in meat, fish, poultry, eggs, cheese, lentils, nuts, and seeds.[76]
1905 Scientific development Synthetic isoleucine is originally reported by French chemist Louis Bouveault.[77][78]
1909 Literature American biochemist Thomas Burr Osborne publishes The Vegetable Proteins.[79]
1912 Scientific development Felix Ehrlich demonstrates that yeast metabolizes the natural amino acids essentially by splitting off carbon dioxide and replacing the amino group with a hydroxyl group. By this reaction, tryptophan gives rise to tryptophol.[80]
1914 Scientific development Citrulline is first isolated from watermelon by Japanese researchers Yotaro Koga and Ryo Odake.[81] It is a naturally occurring amino acid.[82] Two commonly seen forms of citrulline seen are citrulline malate and l-citrulline.[83] "L-citrulline boosts nitric oxide production in the body. Nitric oxide helps the arteries relax and work better, which improves blood flow throughout the body. This may be helpful for treating or preventing some diseases."[84] Citrullus vulgaris (watermelon) is the main source. Some other sources that can help to raise levels of L-citrulline include almonds, cocoa, cantaloupe, chickpeas (garbanzo beans), red meats, certain fish including salmon, muskmelons, squash, bitter melons, pumpkins, gourds, walnuts, peanuts and dark chocolate.[85]
1915 Scientific development Around this time, with advances in knowledge of vitamins, it begins to be understood that some of the virtues of foods come from their contribution of these accessory factors rather than from protein.[1]
1921 Scientific development American scientist John Howard Mueller first isolates methionine,[86] an essential amino acid found in many proteins, including those in foods and those found in the tissues and organs of the body.[87][88] An antioxidant, methionine may help protect the body from damage caused by ionizing radiation. It may detoxify harmful substances in the body, such as heavy metals. Methionine may also prevent liver damage from acetaminophen poisoning. These benefits however have not yet been proven through research.[89] Methionine is abundant in turkey, beef, fish, pork, tofu, milk, cheese, nuts, beans, and whole grains like quinoa.[90]
1923 Notable comment Gregor Mendel refers to "the glorification of the albuminous substances" in earlier times, but at the time of writing "the pendulum of enthusiasm about the proteins has swung from one extreme to the other."[1]
1935 Scientific development Jamaican pediatrician Cicely Williams introduces the term Kwashiorkor two years after publishing the disease's first formal description.[91][92] Kwashiorkor is caused by a lack of protein in the diet.[93]
1936 Scientific development Threonine becomes the last of the 20 common proteinogenic amino acids to be discovered. It is discovered by William Cumming Rose,[94] collaborating with Curtis Meyer. The amino acid is named threonine because it is found to be similar in structure to threonic acid, a four-carbon monosaccharide with molecular formula C4H8O5[95]
1939 Scientific development Walter Kempner at Duke University introduces the rice diet, low-protein diet to treat kidney disease. It consists in a daily ration of 2,000 calories of moderate amounts of boiled rice, sucrose and dextrose, and a restricted range of fruit, supplemented with vitamins. Sodium and chloride are restricted to 150mg and 200mg respectively. The rice diet shows remarkable effects on control of edema and hypertension.[96][97]
1948 Literature Melville Sahyun publishes Proteins and Amino Acids in Nutrition, an early book on the topic.[98]
1949 Scientific development The first protein to be sequenced is insulin, by Frederick Sanger, who correctly determines the amino acid sequence of insulin, thus conclusively demonstrating that proteins consist of linear polymers of amino acids rather than branched chains, colloids, or cyclols.[99] Insulin helps regulate blood sugar levels.[100]
1950 Scientific development Protein becomes a matter of nutritional concern as a result of study of the disease, kwashiorkor in young children (usually 6 mo to 2 yr old) first in Africa and then in Jamaica, Central America and else where. This disease, with a high mortality rate, occurs after weaning onto a bulky, low protein diet, and its onset usually follows a bout with diarrhea.[1]
1950 Scientific development American biochemist William Cumming Rose identifies methionine and valine as nutritionally essential amino acids for young adults.[101][102]
1950–1975 "From about 1950 to 1975 the work of the Nutrition Division of FAO was based on the assumption that "deficiency of protein in the diet is the most serious and widespread problem in the world" (24)."[1]
1950–1975 "A downward trend in the successive estimates of protein require ments, particularly for children, over the period 1950-1975"[1]
1954 Literature Adelle Davis publishes Let's Eat Right to Keep Fit, which describes the importance of combining "incomplete" proteins to make "complete" proteins, and advises that any incomplete proteins not complemented within one hour could not be used by the body.[103]
1959 Literature Anthony Albanese publishes Protein and Amino acid nutrition, which describes the state of knowledge concerning the nutrition of proteins and amino acids.[104]
1969 Scientific development Goldman et al. report that high protein intakes (from 6g/kg/day) in low birth weight infants are associated with a condition known as late metabolic acidosis.[105]
1971 Literature Frances Moore Lappé publishes Diet for a Small Planet, which explains how essential amino acids might be obtained from complementary sources in vegetarian nutrition. This book becomes a bestseller.[106]
1975 Literature Both Vogue and American Journal of Nursing carry articles describing the principles and practice of protein combining.[107][108]
1978 Literature The American Chemical Society Division of Agricultural and Foods Chemistry publishes Nutritional Improvement of Food and Feed Proteins.[109]
1979 Scientific development Isner publishes a report of 17 deaths associated with low-quality liquid protein VLCD, due to heart-related causes.[110]
1989 Literature C.A. Barth and E. Schlimme publish Milk Proteins: Nutritional, Clinical, Functional and Technological Aspects, which reviews the state of knowledge and progress of research on food proteins, and in particular, milk proteins.[111]
1990 Literature Raul A. Wapnir publishes Protein Nutrition and Mineral Absorption, which presents information regarding the mechanisms of protein absorption under normal and pathologic conditions, in addition to reviewing changes that occur at various stages of life.[112]
1993 The Protein Digestibility Corrected Amino Acid Score (PDCAAS) is adopted by the US Food and Drug Administration (FDA) and the Food and Agricultural Organization of the United Nations/World Health Organization (FAO/WHO) as "the preferred 'best'" method to determine protein quality. These organizations suggest that other methods for evaluating the quality of protein are inferior.[113]
1994 Scientific development Vernon Young and Peter Pellett publish their paper that becomes the definitive contemporary guide to protein metabolism in humans. It also confirms that complementing proteins at meals is totally unnecessary. Thus, people who avoid consuming animal protein do not need to be at all concerned about amino acid imbalances from the plant proteins that make up their usual diets.[114]
1994 Literature Zdzisław Sikorski, Bonnie Sun Pan, and Fereidoon Shahidi publish Seafood Proteins, a presentation of the state of knowledge on seafood nitrogenous compounds.[115]
1995 Literature Clarence B. Ammerman, David P. Baker, and Austin J. Lewis publish Bioavailability of Nutrients for Animals: Amino Acids, Minerals, Vitamins, which attempts to provide information necessary to formulate diets with appropriate amounts of amino acids, minerals, and vitamins.[116]
2000 Scientific development The term proteopathy is first proposed by Lary Walker and Harry LeVine.[117] It refers to a disease characterized by the production of aberrant conformers of certain proteins that are misfolded and aggregate in a crystallization-like seeding mechanism—changes that lead to a disturbance of their cellular functions and disease.[118]
2000 Scientific development Brunton et al. show that the gut has a major effect on amino-acid metabolism.[105]
2002 Recommendation The U.S. Institute of Medicine sets a Recommended Dietary Allowance (RDA) of 5 mg/kg body weight/day of Tryptophan for adults 19 years and over.[119] United States
2002 Notable comment American physician Dr. John McDougall writes a correction to the American Heart Association for a 2001 publication that questions the completeness of plant proteins, and further asserts that "it is impossible to design an amino acid–deficient diet based on the amounts of unprocessed starches and vegetables sufficient to meet the calorie needs of humans."[120]
2004 Literature Rickey Y. Yada publshes Proteins in Food Processing, which reviews how proteins may be used to enhance the nutritional, textural and other qualities of food products.[121]
2005 Notable comment Dr. Joel Fuhrman writes:
...plant foods have plenty of protein and you do not have to be a nutritional scientist or dietitian to figure out what to eat and you don’t need to mix and match foods to achieve protein completeness. Any combination of natural foods will supply you with adequate protein, including all eight essential amino acids as well as unessential amino acids.[122]
2006 Notable comment Dr. T. Colin Campbell writes:
We now know that through enormously complex metabolic systems, the human body can derive all the essential amino acids from the natural variety of plant proteins that we encounter every day. It doesn’t require eating higher quantities of plant protein or meticulously planning every meal.[123]
2007 Recommendation Isotope studies and reappraisal of nitrogen balance literature using nonlinear regression suggest that the WHO 2007 (Report of a Joint WHO/FAO/UNU Expert Consultation, 2007) estimates of adult protein requirements are too low, by a factor of around 30%.[105]
2009 Notable comment The American Dietetic Association writes:
Plant protein can meet protein requirements when a variety of plant foods is consumed and energy needs are met. Research indicates that an assortment of plant foods eaten over the course of a day can provide all essential amino acids and ensure adequate nitrogen retention and use in healthy adults, thus, complementary proteins do not need to be consumed at the same meal.[124]
2011 Scientific development A review concludes that a "long-term effect of high-protein diets is neither consistent nor conclusive."[125]
2011 Literature G. O. Phillips and P. A. Williams publish their Handbook of Food Proteins, which provides an overview of the characteristics, functionalities and applications of different proteins of importance to the food industry.[126]
2014 Scientific development A review notes that high-protein diets from animal sources should be handled with caution.[127]
2015–2020 Recommendation The 2015–2020 Dietary Guidelines for Americans (DGA) recommends that men and teenage boys increase their consumption of fruits, vegetables and other under-consumed foods, and that a means of accomplishing this would be to reduce overall intake of protein foods.[128]
2016 Notable comment The American Heart Association states:
You don’t need to eat foods from animals to have enough protein in your diet. Plant proteins alone can provide enough of the essential and non-essential amino acids, as long as sources of dietary protein are varied and caloric intake is high enough to meet energy needs. Whole grains, legumes, vegetables, seeds and nuts all contain both essential and non-essential amino acids. You don’t need to consciously combine these foods (“complementary proteins”) within a given meal.[129]
2017 Scientific development A review indicates that a high-protein diet may contribute to life-long risk of kidney damage, including chronic kidney disease.[130]
2020 Scientific development A review finds that a high-protein diet does not significantly improve blood pressure and glycemic control in people with diabetes.[131]

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