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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. 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.

  4. Ankyrin - Wikipedia

    en.wikipedia.org/wiki/Ankyrin

    The interactions the sites use to bind to membrane proteins are non-specific and consist of: hydrogen bonding, hydrophobic interactions and electrostatic interactions. These non-specific interactions give ankyrin the property to recognise a large range of proteins as the sequence doesn't have to be conserved, just the properties of the amino ...

  5. 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

  6. 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 ...

  7. Protein domain - Wikipedia

    en.wikipedia.org/wiki/Protein_domain

    The primary structure (string of amino acids) of a protein ultimately encodes its uniquely folded three-dimensional (3D) conformation. [20] The most important factor governing the folding of a protein into 3D structure is the distribution of polar and non-polar side chains. [21]

  8. 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)

  9. Protein contact map - Wikipedia

    en.wikipedia.org/wiki/Protein_contact_map

    A protein contact map represents the distance between all possible amino acid residue pairs of a three-dimensional protein structure using a binary two-dimensional matrix. For two residues i {\displaystyle i} and j {\displaystyle j} , the i j {\displaystyle ij} element of the matrix is 1 if the two residues are closer than a predetermined ...