What can Disulfide Bonds Tell Us about Protein Energetics, Function and Folding: Simulations and Bioninformatics Analysis
- 1 July 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 300 (4) , 975-985
- https://doi.org/10.1006/jmbi.2000.3893
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- The transition state in the folding-unfolding reaction of four species of three-disulfide variant of hen lysozyme: the role of each disulfide bridgeJournal of Molecular Biology, 2000
- Universally conserved positions in protein folds: reading evolutionary signals about stability, folding kinetics and functionJournal of Molecular Biology, 1999
- Structure of the transition state in the folding process of human procarboxypeptidase A2 activation domainJournal of Molecular Biology, 1998
- Temperature dependence of the folding rate in a simple protein model: Search for a “glass” transitionThe Journal of Chemical Physics, 1998
- Domains in folding of model proteinsProtein Science, 1995
- How does a protein fold?Nature, 1994
- The folding of an enzyme: IV. Structure of an intermediate in the refolding of barnase analysed by a protein engineering procedureJournal of Molecular Biology, 1992
- Protein folding bottlenecks: A lattice Monte Carlo simulationPhysical Review Letters, 1991
- Conformational Studies by 1H Nuclear Magnetic Resonance of the Basic Pancreatic Trypsin Inhibitor after Reduction of the Disulfide Bond between Cys‐14 and Cys‐38European Journal of Biochemistry, 1979
- Immunochemical analysis of the conformational properties of intermediates trapped in the folding and unfolding of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1978