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Propensities for the formation of individual disulfide bonds in hen lysozyme and the size and stability of disulfide‐associated submolecular structures
Author(s) -
Tachibana Hideki
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(00)01904-9
Subject(s) - lysozyme , chemistry , disulfide bond , circular dichroism , protein disulfide isomerase , crystallography , thiol , urea , molecule , protein structure , stereochemistry , biochemistry , organic chemistry
Hen lysozyme single‐disulfide variants were constructed to characterize the structures associated with the formation of individual native disulfide bonds. Circular dichroism spectra and the effective concentration of protein thiol groups showed that the propensity for structure formation was relatively high for Cys‐6–Cys‐127 and Cys‐30–Cys‐115 disulfides. The urea concentration dependence of individual effective concentrations showed that the apparent sizes of the structures were 14–50% of the whole molecule. The intrinsic stability of each submolecular structure in a reduced form of protein, obtained by subtracting the entropic contribution of cross‐linking, was highest for Cys‐64–Cys‐80 and lowest for Cys‐76–Cys‐94 disulfide bonds.