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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] Only these 22 appear in the genetic code of life ...

  3. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    The alpha helix is also commonly called a: Pauling–Corey–Branson α-helix (from the names of three scientists who described its structure); 3.6 13-helix because there are 3.6 amino acids in one ring, with 13 atoms being involved in the ring formed by the hydrogen bond (starting with amidic hydrogen and ending with carbonyl oxygen)

  4. Absolute configuration - Wikipedia

    en.wikipedia.org/wiki/Absolute_configuration

    A rule of thumb for determining the D/L isomeric form of an amino acid is the "CORN" rule. The groups COOH, R, NH 2 and H (where R is the side-chain) are arranged around the chiral center carbon atom. With the hydrogen atom away from the viewer, if the arrangement of the CO→R→N groups around the carbon atom as center is counter-clockwise ...

  5. Protein primary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_primary_structure

    A phosphate group can be attached to the sidechain hydroxyl group of serine, threonine and tyrosine residues, adding a negative charge at that site and producing an unnatural amino acid. Such reactions are catalyzed by kinases and the reverse reaction is catalyzed by phosphatases.

  6. N-terminus - Wikipedia

    en.wikipedia.org/wiki/N-terminus

    Each amino acid has an amine group and a carboxylic group. Amino acids link to one another by peptide bonds which form through a dehydration reaction that joins the carboxyl group of one amino acid to the amine group of the next in a head-to-tail manner to form a polypeptide chain. The chain has two ends – an amine group, the N-terminus, and ...

  7. Protein metabolism - Wikipedia

    en.wikipedia.org/wiki/Protein_metabolism

    If the pH drops, some amino acids in the polypeptide chain can become protonated if the pka of their R groups is higher than the new pH. Protonation can change the charge these R groups have. If the pH raises, some amino acids in the chain can become deprotonated (if the pka of the R group is lower than the new pH). This also changes the R ...

  8. Category:Amino acids - Wikipedia

    en.wikipedia.org/wiki/Category:Amino_acids

    An amino acid is any molecule that contains both amino and carboxylic acid functional groups. Subcategories This category has the following 18 subcategories, out of 18 total.

  9. 310 helix - Wikipedia

    en.wikipedia.org/wiki/310_helix

    The amino acids in a 3 10-helix are arranged in a right-handed helical structure. Each amino acid corresponds to a 120° turn in the helix (i.e., the helix has three residues per turn), and a translation of 2.0 Å (0.20 nm) along the helical axis, and has 10 atoms in the ring formed by making the hydrogen bond.