Structural analysis of denaturant-protein interactions: comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozyme.

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TitleStructural analysis of denaturant-protein interactions: comparison between the effects of bromoethanol and SDS on denaturation and renaturation of triclinic lysozyme.
Publication TypeJournal Article
Year of Publication1977
AuthorsYonath, A, Podjarny, A, Honig, B, Traub, W, Sielecki, A, Herzberg, O, Moult, J
JournalBiophys Struct Mech
Volume4
Issue1
Pagination27-36
Date Published1977 Dec 27
ISSN0340-1057
KeywordsEthanol, Muramidase, Protein Conformation, Protein Denaturation, Sodium Dodecyl Sulfate, X-Ray Diffraction
Abstract

This paper summarizes our crystallographic studies of the interaction of denaturants with cross-linked triclinic lysozyme. Electron density maps of various bromoethanol-lysozyme complexes are analyzed and compared to those reported earlier for SDS-lysozyme complexes. Despite differences in the chemical nature and size of the two denaturants their mode of interaction with the protein is quite similar, suggesting the existence of a general mechanism for binding of hydrophobic-hydrophilic denaturants to proteins. Our results are consistent with the conclusion that lysozyme consists of two domains connected by a flexible segment and that this segment represents an internal degree of freedom of the protein.

Alternate JournalBiophys. Struct. Mech.
PubMed ID597569