hsp90: Twist and Fold
Copyright policy )hsp90: Twist and Fold
Molecular chaperones are cellular machines that facilitate protein folding. The crystal structures of HtpG, the Escherichia coli homolog of hsp90, reported in this issue (Shiau et al., 2006) together with the recently published structures of an hsp90-cochaperone complex (Ali et al., 2006) and an hsp90-client protein complex (Vaughan et al., 2006), reveal exciting insights into the hsp90 reaction cycle.
- Technical University of Munich Germany
Models, Molecular, Protein Folding, Binding Sites, Biochemistry, Genetics and Molecular Biology(all), Adenine Nucleotides, Protein Conformation, Escherichia coli Proteins, HSP90 Heat-Shock Proteins, Dimerization, Protein Binding
Models, Molecular, Protein Folding, Binding Sites, Biochemistry, Genetics and Molecular Biology(all), Adenine Nucleotides, Protein Conformation, Escherichia coli Proteins, HSP90 Heat-Shock Proteins, Dimerization, Protein Binding
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