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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. 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 ...

  4. 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).

  5. 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.

  6. Isoelectric point - Wikipedia

    en.wikipedia.org/wiki/Isoelectric_point

    If the pH of the buffer is below the pI of the protein being run, the protein will migrate to the negative pole of the gel (positive charge is attracted to the negative pole). If the protein is run with a buffer pH that is equal to the pI, it will not migrate at all. This is also true for individual amino acids.

  7. Sørensen formol titration - Wikipedia

    en.wikipedia.org/wiki/Sørensen_formol_titration

    The Sørensen formol titration(SFT) invented by S. P. L. Sørensen in 1907 [1] is a titration of an amino acid with potassium hydroxide in the presence of formaldehyde. [2] It is used in the determination of protein content in samples. [3] Formol titration equation for amino acids in general

  8. Ramachandran plot - Wikipedia

    en.wikipedia.org/wiki/Ramachandran_plot

    In practice, the major effect seen is that of the presence or absence of the methylene group at Cβ. [5] Glycine has only a hydrogen atom for its side chain, with a much smaller van der Waals radius than the CH 3 , CH 2 , or CH group that starts the side chain of all other amino acids.

  9. Charge transfer coefficient - Wikipedia

    en.wikipedia.org/wiki/Charge_transfer_coefficient

    Charge transfer coefficient, and symmetry factor (symbols α and β, respectively) are two related parameters used in description of the kinetics of electrochemical reactions. They appear in the Butler–Volmer equation and related expressions.