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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Vydáno v:	FEBS letters Ročník 480; číslo 2; s. 175 - 178
Hlavní autor:	Tachibana, Hideki
Médium:	Journal Article
Jazyk:	angličtina
Vydáno:	England Elsevier B.V 01.09.2000
Témata:	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
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Shrnutí:	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.
Bibliografie:	ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23
ISSN:	0014-5793 1873-3468
DOI:	10.1016/S0014-5793(00)01904-9