Copper-Triggered β-Hairpin Formation: Initiation Site for Azurin Folding?
- 16 June 2000
- journal article
- research article
- Published by American Chemical Society (ACS) in Journal of the American Chemical Society
- Vol. 122 (26) , 6337-6338
- https://doi.org/10.1021/ja0011010
Abstract
No abstract availableThis publication has 17 references indexed in Scilit:
- Thermodynamics of a β-hairpin structure: evidence for cooperative formation of folding nucleusJournal of Molecular Biology, 2000
- Conformational analysis of a set of peptides corresponding to the entire primary sequence of the N-terminal domain of the ribosomal protein L9: evidence for stable native-like secondary structure in the unfolded stateJournal of Molecular Biology, 1999
- Reduction potentials of blue and purple copper proteins in their unfolded states: a closer look at rack-induced coordinationJBIC Journal of Biological Inorganic Chemistry, 1998
- Design of a 20-Amino Acid, Three-Stranded β-Sheet ProteinScience, 1998
- Formation and stability of β-hairpin structures in polypeptidesCurrent Opinion in Structural Biology, 1998
- Rate of Intrachain Diffusion of Unfolded Cytochrome cThe Journal of Physical Chemistry B, 1997
- Helix design, prediction and stabilityCurrent Opinion in Biotechnology, 1995
- Folding of peptide fragments comprising the complete sequence of proteinsJournal of Molecular Biology, 1992
- Scaling Population Density to Body Size in Rocky Intertidal CommunitiesScience, 1990
- Computer Simulations of Globular Protein Folding and Tertiary StructureAnnual Review of Physical Chemistry, 1989