Following co-operative formation of secondary and tertiary structure in a single protein module
- 25 April 1997
- journal article
- research article
- Published by Elsevier BV in Journal of Molecular Biology
- Vol. 268 (1), 185-197
- https://doi.org/10.1006/jmbi.1997.0932
Abstract
No abstract availableKeywords
This publication has 38 references indexed in Scilit:
- Structure of the Transition State for Folding of a Protein Derived from Experiment and SimulationJournal of Molecular Biology, 1996
- Conformational Pathway of the Polypeptide Chain of Chymotrypsin Inhibitor-2 Growing from its N Terminusin vitro. Parallels with the Protein Folding PathwayJournal of Molecular Biology, 1995
- Folding of a nascent polypeptide chain in vitro: cooperative formation of structure in a protein module.Proceedings of the National Academy of Sciences of the United States of America, 1995
- The structure of the transition state for the association of two fragments of the barley chymotrypsin inhibitor 2 to generate native-like protein: implications for mechanisms of protein folding.Proceedings of the National Academy of Sciences of the United States of America, 1994
- Generation of a Family of Protein Fragments for Structure-folding Studies. 2. Kinetics of Association of the Two Chymotrypsin Inhibitor-2 FragmentsBiochemistry, 1994
- Generation of a Family of Protein Fragments for Structure-Folding Studies. 1. Folding Complementation of Two Fragments of Chymotrypsin Inhibitor-2 Formed by Cleavage at Its Unique Methionine ResidueBiochemistry, 1994
- Cooperativity in protein-folding kinetics.Proceedings of the National Academy of Sciences, 1993
- Comparison of the solution and X-ray structures of barley serine proteinase inhibitor 2Protein Engineering, Design and Selection, 1987
- The determination of the three-dimensional structure of barley serine proteinase inhibitor 2 by nuclear magnetic resonance, distance geometry and restrained molecular dynamicsProtein Engineering, Design and Selection, 1987
- Principles that Govern the Folding of Protein ChainsScience, 1973