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  2. Casein - Wikipedia

    en.wikipedia.org/wiki/Casein

    Sheep and cow milk have a higher casein content than other types of milk with human milk having a particularly low casein content. [2] Casein is the primary emulsifier in milk, that is, it helps in mixing oils, fats, and water in milk. [3] Casein has a wide variety of uses, from being a major component of cheese, to use as a food additive. [4]

  3. Eating More Protein to Lose Weight? Avoid These 6 Common Mistakes

    www.aol.com/eating-more-protein-lose-weight...

    “Spreading protein intake across the day helps keep a constant flow of amino acids to your muscles,” said Christopher Mohr, PhD, RDN, a registered dietitian and fitness and nutrition advisor ...

  4. Glycine - Wikipedia

    en.wikipedia.org/wiki/Glycine

    Glycine (symbol Gly or G; [6] / ˈ ɡ l aɪ s iː n / ⓘ) [7] is an amino acid that has a single hydrogen atom as its side chain. It is the simplest stable amino acid (carbamic acid is unstable). Glycine is one of the proteinogenic amino acids. It is encoded by all the codons starting with GG (GGU, GGC, GGA, GGG). [8]

  5. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    It is a conditionally essential amino acid with a polar side group. The word "tyrosine" is from the Greek tyrós, meaning cheese, as it was first discovered in 1846 by German chemist Justus von Liebig in the protein casein from cheese. [3] [4] It is called tyrosyl when referred to as a functional group or side chain.

  6. Whey - Wikipedia

    en.wikipedia.org/wiki/Whey

    Whey protein has a high level of leucine, [21] one of the three branched-chain amino acids, making it ideal for muscle growth and repair. [citation needed] [22] Whey is pasteurized to assure that no harmful bacteria are breeding in the liquid. It is heated to 70–80 °C (158–176 °F) and is then cooled back down to 4 °C (39 °F).

  7. Tryptophan - Wikipedia

    en.wikipedia.org/wiki/Tryptophan

    Like other amino acids, tryptophan is a zwitterion at physiological pH where the amino group is protonated (– NH + 3; pK a = 9.39) and the carboxylic acid is deprotonated ( –COO −; pK a = 2.38). [5] Humans and many animals cannot synthesize tryptophan: they need to obtain it through their diet, making it an essential amino acid.

  8. Complete protein - Wikipedia

    en.wikipedia.org/wiki/Complete_protein

    The foodstuffs listed for comparison show the essential amino acid content per unit of the total protein of the food, 100g of spinach, for example, only contains 2.9g of protein (6% Daily Value), and of that protein 1.36% is tryptophan. [2] [7] (note that the examples have not been corrected for digestibility)

  9. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Amino acids can have multiple codons that correspond to them. Ribosomes do not directly attach amino acids to mRNA codons. They must utilize tRNAs (transfer RNAs) as well. Transfer RNAs can bind to amino acids and contain an anticodon which can hydrogen bind to an mRNA codon. [13] The process of bind an amino acid to a tRNA is known as tRNA ...