Is protein folding hierarchic? II. Folding intermediates and transition states
Open Access
- 1 February 1999
- journal article
- review article
- Published by Elsevier in Trends in Biochemical Sciences
- Vol. 24 (2) , 77-83
- https://doi.org/10.1016/s0968-0004(98)01345-0
Abstract
No abstract availableKeywords
This publication has 48 references indexed in Scilit:
- A specific hydrophobic core in the α-lactalbumin molten globuleJournal of Molecular Biology, 1998
- The changing nature of the protein folding transition state: implications for the shape of the free-energy profile for foldingJournal of Molecular Biology, 1998
- Folding intermediates of wild-type and mutants of barnase. I. use of φ-value analysis and m-values to probe the cooperative nature of the folding pre-equilibriumJournal of Molecular Biology, 1998
- Native tertiary structure in an A-stateJournal of Molecular Biology, 1998
- Three-state model for lysozyme folding: triangular folding mechanism with an energetically trapped intermediateJournal of Molecular Biology, 1997
- Native-like β-structure in a Trifluoroethanol-induced Partially Folded State of the All-β-sheet Protein TendamistatJournal of Molecular Biology, 1996
- 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
- Rapid formation of secondary structure framework in protein folding studied by stopped‐flow circular dichroismFEBS Letters, 1987
- Evidence for identity between the equilibrium unfolding intermediate and a transient folding intermediate: a comparative study of the folding reactions of .alpha.-lactalbumin and lysozymeBiochemistry, 1986
- A Native‐Like Intermediate on the Ribonuclease A Folding PathwayEuropean Journal of Biochemistry, 1981