Characterization of a molten globule intermediate during GdnHCl-induced unfolding of RTEM β-lactamase from Escherichia coli
- 15 August 1996
- journal article
- Published by Elsevier in Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology
- Vol. 1296 (1) , 85-94
- https://doi.org/10.1016/0167-4838(96)00056-8
Abstract
No abstract availableKeywords
This publication has 27 references indexed in Scilit:
- "Partly Folded" State, a New Equilibrium State of Protein Molecules: Four-State Guanidinium Chloride-Induced Unfolding of .beta.-Lactamase at Low TemperatureBiochemistry, 1994
- Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediateBiochemistry, 1993
- ‘All‐or‐none’ mechanism of the molten globule unfoldingFEBS Letters, 1992
- A protein-folding reaction under kinetic controlNature, 1992
- INTERMEDIATES IN THE FOLDING REACTIONS OF SMALL PROTEINSAnnual Review of Biochemistry, 1990
- Evidence for a molten globule state as a general intermediate in protein foldingFEBS Letters, 1990
- Location of the active sites of some enzymes in limited and flexible molecular regionsTrends in Biochemical Sciences, 1986
- Detection and characterization of the intermediate on the folding pathway of human .alpha.-lactalbuminBiochemistry, 1978
- Principles that Govern the Folding of Protein ChainsScience, 1973
- Kinetics of unfolding and refolding of proteins: I. Mathematical analysisJournal of Molecular Biology, 1973