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Literature DB >> 8990176

Two-state models of protein folding kinetics.

Abstract

The folding of some proteins appears to be a two-state kinetic process. A two-state kinetic model is justified if protein molecules rapidly equilibrate between different unfolded conformations prior to complete folding. Here I show that this rapid equilibration is a natural consequence of reasonable assumptions about reaction rate constants and folding thermodynamics.

Mesh：

Year: 1997 PMID： 8990176 PMCID： PMC19262 DOI： 10.1073/pnas.94.1.148

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

4 in total

1. The role of solvent viscosity in the dynamics of protein conformational changes.

Authors: A Ansari; C M Jones; E R Henry; J Hofrichter; W A Eaton
Journal: Science Date: 1992-06-26 Impact factor: 47.728

2. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.

Authors: S E Jackson; A R Fersht
Journal: Biochemistry Date: 1991-10-29 Impact factor: 3.162

Review 3. Fast events in protein folding.

Authors: W A Eaton; P A Thompson; C K Chan; S J Hage; J Hofrichter
Journal: Structure Date: 1996-10-15 Impact factor: 5.006

Review 4. Toward a better understanding of protein folding pathways.

Authors: T E Creighton
Journal: Proc Natl Acad Sci U S A Date: 1988-07 Impact factor: 11.205

4 in total

36 in total

Two-state models of protein folding kinetics.

1. The role of solvent viscosity in the dynamics of protein conformational changes.

2. Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition.

Review 3. Fast events in protein folding.

Review 4. Toward a better understanding of protein folding pathways.

1. On the simulation of protein folding by short time scale molecular dynamics and distributed computing.

2. Fast protein folding kinetics.

3. Quantifying internal friction in unfolded and intrinsically disordered proteins with single-molecule spectroscopy.

4. Direct observation of stick-slip movements of water nanodroplets induced by an electron beam.

5. Role of unfolded state heterogeneity and en-route ruggedness in protein folding kinetics.

6. Folding cooperativity in a three-stranded beta-sheet model.

7. Analyzing the biopolymer folding rates and pathways using kinetic cluster method.

8. Master equation approach to finding the rate-limiting steps in biopolymer folding.

9. How long does it take to equilibrate the unfolded state of a protein?

10. Toward a quantitative theory of intrinsically disordered proteins and their function.