Propensities for the formation of individual disulfide bonds in hen lysozyme and the size and stability of disulfide-associated submolecular structures

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 relativ...

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Bibliographic Details
Published in:FEBS letters Vol. 480; no. 2; pp. 175 - 178
Main Author: Tachibana, Hideki
Format: Journal Article
Language:English
Published: England Elsevier B.V 01.09.2000
Subjects:
1SS-n (n=1–4), single-disulfide variant of hen lysozyme that retains SSn
3SS, three-disulfide
Animals
C eff D, effective concentration under denaturing solution conditions
C eff, effective concentration
Cysteine - metabolism
Disulfide bond
Disulfides - chemistry
Effective concentration
Genetic Variation
GSH, reduced glutathione
GSSG, oxidized glutathione
Hen lysozyme
Muramidase - biosynthesis
Muramidase - chemistry
Muramidase - genetics
Oxi, oxidized form of protein
Oxidative folding
Protein Conformation
Red, reduced form of protein
SSn (n=1–4), each of the four native disulfide bonds in hen lysozyme between Cys residues 6–127, 30–115, 64–80, and 76–94, for n=1, 2, 3, and 4, respectively
Sulfhydryl Compounds
Urea
GSH, reduced glutathione
GSSG, oxidized glutathione
SS n ( n=1–4), each of the four native disulfide bonds in hen lysozyme between Cys residues 6–127, 30–115, 64–80, and 76–94, for n=1, 2, 3, and 4, respectively
Red, reduced form of protein
Oxidative folding
C eff D, effective concentration under denaturing solution conditions
3SS, three-disulfide
1SS- n ( n=1–4), single-disulfide variant of hen lysozyme that retains SS n
Disulfide bond
Oxi, oxidized form of protein
C eff, effective concentration
Hen lysozyme
Effective concentration
ISSN:0014-5793, 1873-3468
Online Access:Get full text
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Summary: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.
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ISSN:0014-5793
1873-3468
DOI:10.1016/S0014-5793(00)01904-9