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  2. Protein (nutrient) - Wikipedia

    en.wikipedia.org/wiki/Protein_as_nutrient

    Absorption of the amino acids and their derivatives into which dietary protein is degraded is done by the gastrointestinal tract. The absorption rates of individual amino acids are highly dependent on the protein source; for example, the digestibilities of many amino acids in humans, the difference between soy and milk proteins [32] and between ...

  3. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The common natural forms of amino acids have a zwitterionic structure, with −NH + 3 (−NH + 2 − in the case of proline) and −CO − 2 functional groups attached to the same C atom, and are thus α-amino acids, and are the only ones found in proteins during translation in the ribosome.

  4. Protein - Wikipedia

    en.wikipedia.org/wiki/Protein

    The side chains of the standard amino acids have a variety of chemical structures and properties, and it is the combined effect of all amino acids that determines its three-dimensional structure and chemical reactivity. [35] The amino acids in a polypeptide chain are linked by peptide bonds between amino and carboxyl

  5. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    Protein anabolism is the process by which proteins are formed from amino acids. It relies on five processes: amino acid synthesis, transcription, translation, post translational modifications, and protein folding. Proteins are made from amino acids. In humans, some amino acids can be synthesized using already existing intermediates. These amino ...

  6. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    Protein primary structure is the linear sequence of amino acids in a peptide or protein. [1] By convention, the primary structure of a protein is reported starting from the amino-terminal (N) end to the carboxyl-terminal (C) end. Protein biosynthesis is most commonly performed by ribosomes in cells. Peptides can also be synthesized in the ...

  7. Glycoprotein - Wikipedia

    en.wikipedia.org/wiki/Glycoprotein

    Within the cell, they appear in the blood, the extracellular matrix, or on the outer surface of the plasma membrane, and make up a large portion of the proteins secreted by eukaryotic cells. [4] They are very broad in their applications and can function as a variety of chemicals from antibodies to hormones.

  8. Glutamine - Wikipedia

    en.wikipedia.org/wiki/Glutamine

    Glutamine plays a role in a variety of biochemical functions: Protein synthesis, as any other of the 20 proteinogenic amino acids; Lipid synthesis, especially by cancer cells. [8] Regulation of acid-base balance in the kidney by producing ammonium [9] Cellular energy, as a source, next to glucose [10]

  9. Proteolysis - Wikipedia

    en.wikipedia.org/wiki/Proteolysis

    Proteins in cells are broken into amino acids. This intracellular degradation of protein serves multiple functions: It removes damaged and abnormal proteins and prevents their accumulation. It also serves to regulate cellular processes by removing enzymes and regulatory proteins that are no longer needed.