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

doi:10.1016/s0014-5793(00)01904-9

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Article

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

FEBS letters - 1 Sept 2000

Tachibana H

Abstract excerpt

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...

Topics

Animals
Cysteine
Disulfides
Genetic Variation
Muramidase
Protein Conformation
Sulfhydryl Compounds
Urea

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PMID: 11034323
DOI: 10.1016/s0014-5793(00)01904-9

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