Topology, Stability, Sequence, and Length: Defining the Determinants of Two-State Protein Folding Kinetics
Top Cited Papers
- 25 August 2000
- journal article
- review article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 39 (37) , 11177-11183
- https://doi.org/10.1021/bi000200n
Abstract
No abstract availableKeywords
This publication has 13 references indexed in Scilit:
- Submillisecond folding of the peripheral subunit-binding domainJournal of Molecular Biology, 1999
- Mapping the Interactions Present in the Transition State for Unfolding/Folding of FKBP12Journal of Molecular Biology, 1999
- Rapid folding with and without populated intermediates in the homologous four-helix proteins Im7 and Im9Journal of Molecular Biology, 1999
- Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Contact order, transition state placement and the refolding rates of single domain proteins 1 1Edited by P. E. WrightJournal of Molecular Biology, 1998
- Folding kinetics of the SH3 domain of PI3 kinase by real-time NMR combined with optical spectroscopyJournal of Molecular Biology, 1998
- Pathways for protein folding: is a new view needed?Current Opinion in Structural Biology, 1998
- THEORY OF PROTEIN FOLDING: The Energy Landscape PerspectiveAnnual Review of Physical Chemistry, 1997
- A comparison of the folding kinetics and thermodynamics of two homologous fibronectin type III modulesJournal of Molecular Biology, 1997
- Fast and One-step Folding of Closely and Distantly Related Homologous Proteins of a Four-helix Bundle FamilyJournal of Molecular Biology, 1996