Biophysics of structure and mechanism

, Volume 4, Issue 1, pp 27–36

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

Authors

  • Ada Yonath
    • Department of Structural ChemistryWeizmann Institute of Science
  • Alberto Podjarny
    • Department of Structural ChemistryWeizmann Institute of Science
  • Barry Honig
    • Department of Physical ChemistryThe Hebrew University of Jerusalem
  • Wolfie Traub
    • Department of Structural ChemistryWeizmann Institute of Science
  • Anita Sielecki
    • Department of Structural ChemistryWeizmann Institute of Science
  • Osnat Herzberg
    • Department of Structural ChemistryWeizmann Institute of Science
  • John Moult
    • Department of Structural ChemistryWeizmann Institute of Science
Article

DOI: 10.1007/BF00538838

Cite this article as:
Yonath, A., Podjarny, A., Honig, B. et al. Biophys. Struct. Mechanism (1978) 4: 27. doi:10.1007/BF00538838

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.

Key words

DenaturationRenaturationProteins (Lysozyme)

Copyright information

© Springer-Verlag 1978