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  2. Amino acid score - Wikipedia

    en.wikipedia.org/wiki/Amino_acid_score

    Amino acids are composed of a side chain , a basic amino group, and a carboxyl group. Based on an aminos R group every amino acid will react different because of shape or composition. They can be divided into four different groups non polar amino acids, polar amino acids, positively charged, and negatively charged R group.

  3. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    prot pi – protein isoelectric point — an online program for calculating pI of proteins (include multiple subunits and posttranslational modifications) CurTiPot — a suite of spreadsheets for computing acid-base equilibria (charge versus pH plot of amphoteric molecules e.g., amino acids)

  4. Hydrophobicity scales - Wikipedia

    en.wikipedia.org/wiki/Hydrophobicity_scales

    Also, amino acid side chain affinity for water was measured using vapor phases. [14] Vapor phases represent the simplest non polar phases, because it has no interaction with the solute. [18] The hydration potential and its correlation to the appearance of amino acids on the surface of proteins was studied by Wolfenden.

  5. Amino acid - Wikipedia

    en.wikipedia.org/wiki/Amino_acid

    Five amino acids possess a charge at neutral pH. Often these side chains appear at the surfaces on proteins to enable their solubility in water, and side chains with opposite charges form important electrostatic contacts called salt bridges that maintain structures within a single protein or between interfacing proteins. [32]

  6. Protein pKa calculations - Wikipedia

    en.wikipedia.org/wiki/Protein_pKa_calculations

    FDPB-based methods calculate the change in the pK a value of an amino acid side chain when that side chain is moved from a hypothetical fully solvated state to its position in the protein. To perform such a calculation, one needs theoretical methods that can calculate the effect of the protein interior on a p K a value, and knowledge of the pKa ...

  7. Salt bridge (protein and supramolecular) - Wikipedia

    en.wikipedia.org/wiki/Salt_bridge_(protein_and...

    The N-O distance required is less than 4 Å (400 pm). Amino acids greater than this distance apart do not qualify as forming a salt bridge. [11] Due to the numerous ionizable side chains of amino acids found throughout a protein, the pH at which a protein is placed is crucial to its stability.

  8. De novo peptide sequencing - Wikipedia

    en.wikipedia.org/wiki/De_novo_peptide_sequencing

    Mass of b 2-ions are listed in Table 2, as well as single amino acids that have equal mass to b 2-ions. [15] The mass of b 2-ion = mass of two amino acid residues + 1. Table 2. Mass of b2-ions in peptide fragmentation [16] Identify a sequence ion series by the same mass difference, which matches one of the amino acid residue masses (see Table 1).

  9. Conservative replacement - Wikipedia

    en.wikipedia.org/wiki/Conservative_replacement

    A conservative replacement (also called a conservative mutation or a conservative substitution or a homologous replacement) is an amino acid replacement in a protein that changes a given amino acid to a different amino acid with similar biochemical properties (e.g. charge, hydrophobicity and size). [1] [2]