Characterizing transition states in protein folding: an essential step in the puzzle
- 1 February 1995
- journal article
- review article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 5 (1) , 79-84
- https://doi.org/10.1016/0959-440x(95)80012-p
Abstract
No abstract availableKeywords
This publication has 17 references indexed in Scilit:
- The folding of an enzyme: I. Theory of protein engineering analysis of stability and pathway of protein foldingPublished by Elsevier ,2004
- Roles of molecular chaperones in protein foldingCurrent Opinion in Structural Biology, 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
- How does a protein fold?Nature, 1994
- Refolding of Barnase in the Presence of GroEJournal of Molecular Biology, 1993
- Protein folding and stability: the pathway of folding of barnaseFEBS Letters, 1993
- Protein Folding Studied Using Hydrogen-Exchange Labeling and Two-Dimensional NMRAnnual Review of Biophysics, 1992
- The folding of an enzyme: III. Structure of the transition state for unfolding of barnase analysed by a protein engineering procedureJournal of Molecular Biology, 1992
- 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