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  2. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    The pH-dependence of the activity displayed by enzymes and the pH-dependence of protein stability, for example, are properties that are determined by the pK a values of amino acid side chains. The p K a values of an amino acid side chain in solution is typically inferred from the p K a values of model compounds (compounds that are similar to ...

  3. AAindex - Wikipedia

    en.wikipedia.org/wiki/AAindex

    AAindex is a database of amino acid indices, amino acid mutation matrices, and pair-wise contact potentials. [ 1 ] [ 2 ] The data represent various physicochemical and biochemical properties of amino acids and pairs of amino acids.

  4. List of amino acids - Wikipedia

    en.wikipedia.org/wiki/List_of_amino_acids

    Amino acids are listed by type: Proteinogenic amino acid; Non-proteinogenic amino acids This page was last edited on 5 ...

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    The two amino acid residues are linked through a peptide bond. As both the amine and carboxylic acid groups of amino acids can react to form amide bonds, one amino acid molecule can react with another and become joined through an amide linkage. This polymerization of amino acids is what creates proteins.

  6. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    The first and third scales are derived from the physiochemical properties of the amino acid side chains. These scales result mainly from inspection of the amino acid structures. [14] [1] Biswas et al., divided the scales based on the method used to obtain the scale into five different categories. [3]

  7. Amino acid score - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_score

    By using an amino acid score, it can be indicated if a protein will meet all amino acid needs of the body. If the amino acid score meets the required score it will be a completed or ideal protein. To calculate the amino acid score the formula used is, the milligram of limiting amino acid in 1 gram of test protein/ the milligram of that same ...

  8. Protein structure prediction - Wikipedia

    en.wikipedia.org/wiki/Protein_structure_prediction

    An alpha-helix with hydrogen bonds (yellow dots) The α-helix is the most abundant type of secondary structure in proteins. The α-helix has 3.6 amino acids per turn with an H-bond formed between every fourth residue; the average length is 10 amino acids (3 turns) or 10 Å but varies from 5 to 40 (1.5 to 11 turns).

  9. BLOSUM - Wikipedia

    en.wikipedia.org/wiki/BLOSUM

    However, these amino acids can be categorised into groups with similar physicochemical properties. [5] Substituting an amino acid with another from the same category is more likely to have a smaller impact on the structure and function of a protein than replacement with an amino acid from a different category.