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Aspartic acid (symbol Asp or D; [4] the ionic form is known as aspartate), is an α-amino acid that is used in the biosynthesis of proteins. [5] The L-isomer of aspartic acid is one of the 22 proteinogenic amino acids, i.e., the building blocks of proteins. D-aspartic acid is one of two D-amino acids commonly found in mammals.
Furthermore, in the folded protein, the aspartic acid will be closer to other titratable groups in the protein and will also interact with permanent charges (e.g. ions) and dipoles in the protein. All of these effects alter the p K a value of the amino acid side chain, and p K a calculation methods generally calculate the effect of the protein ...
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A salt bridge in T4 lysozyme between aspartic acid (Asp) at residue 70 and a histidine (His) at residue 31. The contribution of a salt bridge to the overall stability to the folded state of a protein can be assessed through thermodynamic data gathered from mutagenesis studies and nuclear magnetic resonance techniques. [13]
Nitric acid, with a pK value of around −1.7, behaves as a strong acid in aqueous solutions with a pH greater than 1. [23] At lower pH values it behaves as a weak acid. pK a values for strong acids have been estimated by theoretical means. [24] For example, the pK a value of aqueous HCl has been estimated as −9.3.
The value for Arg is from Pace et al. (2009). [7] The value for Sec is from Byun & Kang (2011). [8] N.D.: The pKa value of Pyrrolysine has not been reported. Note: The pKa value of an amino-acid residue in a small peptide is typically slightly different when it is inside a protein.
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For amino acids with charged side chains, the pKa of the side chain is involved. Thus for aspartate or glutamate with negative side chains, the terminal amino group is essentially entirely in the charged form NH, but this positive charge needs to be balanced by the state with just one C-terminal carboxylate group is negatively charged.