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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. Serine - Wikipedia

    en.wikipedia.org/wiki/Serine

    Serine (symbol Ser or S) [3] [4] is an α-amino acid that is used in the biosynthesis of proteins. It contains an α-amino group (which is in the protonated − NH +3 form under biological conditions), a carboxyl group (which is in the deprotonated − COO −

  4. Protein (nutrient) - Wikipedia

    en.wikipedia.org/wiki/Protein_(nutrient)

    Most peptides longer than four amino acids are not absorbed. Absorption into the intestinal absorptive cells is not the end. There, most of the peptides are broken into single amino acids. Absorption of the amino acids and their derivatives into which dietary protein is degraded is done by the gastrointestinal tract.

  5. 10 nutritional deficiencies that can cause depression and ...

    www.aol.com/article/2016/02/05/10-nutritional...

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  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.

  7. Protein folding - Wikipedia

    en.wikipedia.org/wiki/Protein_folding

    This structure is determined by the amino-acid sequence or primary structure. [2] The correct three-dimensional structure is essential to function, although some parts of functional proteins may remain unfolded, [3] indicating that protein dynamics are important. Failure to fold into a native structure generally produces inactive proteins, but ...

  8. Backbone-dependent rotamer library - Wikipedia

    en.wikipedia.org/wiki/Backbone-dependent_rotamer...

    Backbone-dependent rotamer library for serine.Each plot shows the population of the χ 1 rotamers of serine as a function of the backbone dihedral angles φ and ψ. In biochemistry, a backbone-dependent rotamer library provides the frequencies, mean dihedral angles, and standard deviations of the discrete conformations (known as rotamers) of the amino acid side chains in proteins as a function ...

  9. 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