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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., Welfle, K., Misselwitz, R., 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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