Collapse and cooperativity in protein folding
- 1 February 1996
- journal article
- review article
- Published by Elsevier in Current Opinion in Structural Biology
- Vol. 6 (1) , 31-42
- https://doi.org/10.1016/s0959-440x(96)80092-3
Abstract
No abstract availableKeywords
This publication has 77 references indexed in Scilit:
- The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein FoldingJournal of Molecular Biology, 1995
- Extremely rapid protein folding in the absence of intermediatesNature Structural & Molecular Biology, 1995
- Folding of a four-helix bundle: studies of acyl-coenzyme A binding proteinBiochemistry, 1995
- Evidence for a molten globule-like transition state in protein folding from determination of activation volumesBiochemistry, 1995
- Is Burst Hydrophobic Collapse Necessary for Protein Folding?Biochemistry, 1995
- Characterizing transition states in protein folding: an essential step in the puzzleCurrent Opinion in Structural Biology, 1995
- Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2.Proceedings of the National Academy of Sciences, 1994
- Single versus parallel pathways of protein folding and fractional formation of structure in the transition state.Proceedings of the National Academy of Sciences, 1994
- Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding.Proceedings of the National Academy of Sciences, 1994
- Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysisBiochemistry, 1993