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  2. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The 20 amino acids that are encoded directly by the codons of the universal genetic code are called standard or canonical amino acids. A modified form of methionine (N-formylmethionine) is often incorporated in place of methionine as the initial amino acid of proteins in bacteria, mitochondria and plastids (including chloroplasts).

  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 repeating unit of a polymer.

  4. Alpha sheet - Wikipedia

    en.wikipedia.org/wiki/Alpha_sheet

    Alpha sheet (also known as alpha pleated sheet or polar pleated sheet) is an atypical secondary structure in proteins, first proposed by Linus Pauling and Robert Corey in 1951. [1][2][3] The hydrogen bonding pattern in an alpha sheet is similar to that of a beta sheet, but the orientation of the carbonyl and amino groups in the peptide bond ...

  5. Alpha helix - Wikipedia

    en.wikipedia.org/wiki/Alpha_helix

    Alpha helix. Three-dimensional structure of an alpha helix in the protein crambin. An alpha helix (or α-helix) is a sequence of amino acids in a protein that are twisted into a coil (a helix). The alpha helix is the most common structural arrangement in the secondary structure of proteins. It is also the most extreme type of local structure ...

  6. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Hydrophobicity scales. Hydrophobicity scales are values that define the relative hydrophobicity or hydrophilicity of amino acid residues. The more positive the value, the more hydrophobic are the amino acids located in that region of the protein. These scales are commonly used to predict the transmembrane alpha-helices of membrane proteins.

  7. Protein secondary structure - Wikipedia

    en.wikipedia.org/wiki/Protein_secondary_structure

    The first widely used techniques to predict protein secondary structure from the amino acid sequence were the Chou–Fasman method [17] [18] [19] and the GOR method. [20] Although such methods claimed to achieve ~60% accurate in predicting which of the three states (helix/sheet/coil) a residue adopts, blind computing assessments later showed ...

  8. 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 ...

  9. Aromatic amino acid - Wikipedia

    en.wikipedia.org/wiki/Aromatic_amino_acid

    Aromatic amino acids, excepting histidine, absorb ultraviolet light above and beyond 250 nm and will fluoresce under these conditions. This characteristic is used in quantitative analysis, notably in determining the concentrations of these amino acids in solution. [1] [2] Most proteins absorb at 280 nm due to the presence of tyrosine and ...