Open AccessProtein volumes and hydration effects
Author(s) -
PERKINS Stephen J.
Publication year - 1986
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1986.tb09653.x
Subject(s) - chemistry , partial specific volume , residue (chemistry) , amino acid , amino acid residue , neutron scattering , scattering , absorption (acoustics) , crystallography , neutron , analytical chemistry (journal) , peptide sequence , chromatography , biochemistry , physics , optics , enzyme , gene , quantum mechanics
Amino acid sequences, carbohydrate compositions and residue volumes are used to compare critically calculations of partial specific volumes v̄, neutron scattering matchpoints and 280‐nm absorption coefficients with experimental v̄ values for proteins and glycoproteins. The v̄ values that are obtained from amino acid densitometry underestimate experimental v̄ values by 0.01–0.02 ml/g while the v̄ values from crystallographic volumes overestimate the experimental v̄ values by 0.04–0.05 ml/g. An intermediate consensus volume set of amino‐acid‐residue volumes is proposed in order to predict experimental v̄ values using sequence information. The method is extended to carbohydrates and glycoproteins. Neutron scattering matchpoints can be calculated from crystallographic residue volumes on the basis of the non‐exchange of 10% of the main‐chain NH protons. Crystallographic results on protein‐bound water are used to account for the experimental values of v̄ and matchpoints. Finally, 280‐nm absorption coefficients. A 1%,1 cm 280 , of 5–27 are found to be well predicted by the Wetlaufer procedure based on the totals of Trp, Tyr and Cys residues. Average errors are ±0.7, and the experimental A 1%,1 cm 280 values can be larger than the predicted values by 3%.