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...

Full description

Saved in:

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
Tags:	Add Tag No Tags, Be the first to tag this record!

Be the first to leave a comment!