Conformational stability of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis, and of the four HBsu variants [F29W],[F47W],[F50W] and [F79W]

Item Type:	Article
Title:	Conformational stability of the DNA-binding histone-like protein, HBsu, from Bacillus subtilis, and of the four HBsu variants [F29W],[F47W],[F50W] and [F79W]
Creators Name:	Welfle, H. and Welfle, K. and Misselwitz, R. and Groch, N. and Heinemann, U.
Keywords:	Bacillus Subtilis, Bacterial Proteins, Circular Dichroism, DNA-Binding Proteins, Molecular Models, Osmolar Concentration, Point Mutation, Polymerase Chain Reaction, Protein Conformation, Protein Denaturation, Protein Folding, Temperature, Thermodynamics
Source:	Journal of Biomolecular Structure & Dynamics
ISSN:	0739-1102
Volume:	11
Page Range:	381-394
Date:	1 January 1993
PubMed:	View item in PubMed

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