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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Structure of a typical L-alpha-amino acid in the "neutral" form. Amino acids are organic compounds that contain both amino and carboxylic acid functional groups. [1] Although over 500 amino acids exist in nature, by far the most important are the 22 α-amino acids incorporated into proteins. [2]

  3. Protein structure - Wikipedia

    en.wikipedia.org/wiki/Protein_structure

    Protein structure is the three-dimensional arrangement of atoms in an amino acid-chain molecule. Proteins are polymers – specifically polypeptides – formed from sequences of amino acids, which are the monomers of the polymer. A single amino acid monomer may also be called a residue, which indicates a

  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. Collagen - Wikipedia

    en.wikipedia.org/wiki/Collagen

    Hydroxylation of lysine and proline amino acids occurs inside the lumen. This process is dependent on and consumes ascorbic acid (vitamin C) as a cofactor. Glycosylation of specific hydroxylysine residues occurs. Triple alpha helical structure is formed inside the endoplasmic reticulum from two alpha-1 chains and one alpha-2 chain.

  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. Tyrosine - Wikipedia

    en.wikipedia.org/wiki/Tyrosine

    Phosphorylation of these three amino acids' moieties (including tyrosine) creates a negative charge on their ends, that is greater than the negative charge of the only negatively charged aspartic and glutamic acids. Phosphorylated proteins keep these same properties—which are useful for more reliable protein-protein interactions—by means of ...

  8. Arginine - Wikipedia

    en.wikipedia.org/wiki/Arginine

    Arginine is the amino acid with the formula (H 2 N)(HN)CN(H)(CH 2) 3 CH(NH 2)CO 2 H. The molecule features a guanidino group appended to a standard amino acid framework. At physiological pH, the carboxylic acid is deprotonated (−CO 2 −) and both the amino and guanidino groups are

  9. File:Molecular structures of the 21 proteinogenic amino acids ...

    en.wikipedia.org/wiki/File:Molecular_structures...

    Портал:Molecular and cellular biology/Proteinogenic amino acids; Usage on sw.wikipedia.org Asidi amino; Usage on uk.wikipedia.org Амінокислоти; Usage on www.wikidata.org Q8066; Usage on yo.wikipedia.org Àwọn Amino acid; Usage on zh.wikipedia.org 蛋白胺基酸