A diffusion–collision–adhesion model for the kinetics of myoglobin refolding
- 1 August 1980
- journal article
- letter
- Published by Springer Nature in Nature
- Vol. 286 (5773) , 632-634
- https://doi.org/10.1038/286632a0
Abstract
There are two distinct experimental and theoretical problems of protein folding: the thermodynamic issue of characterizing the folded state, and the kinetic question of the path between the unfolded and native states1. Here we consider the second question and present a diffusion–collision–adhesion model for the folding of the α-helical protein myoglobin. In particular, we consider the fast refolding species of the unfolded state and ignore the slow transition between unfolded states that has been attributed to proline isomerization2.Keywords
This publication has 12 references indexed in Scilit:
- Protein folding: Evaluation of some simple rules for the assembly of helices into tertiary structures with myoglobin as an exampleJournal of Molecular Biology, 1979
- Diffusion–collision model for protein foldingBiopolymers, 1979
- Experimental studies of protein folding and unfoldingProgress in Biophysics and Molecular Biology, 1979
- Packing of α-helices: Geometrical constraints and contact areasJournal of Molecular Biology, 1978
- Protein-folding dynamicsNature, 1976
- Consideration of the possibility that the slow step in protein denaturation reactions is due to cis-trans isomerism of proline residuesBiochemistry, 1975
- A model of myoglobin self-organizationBiophysical Chemistry, 1975
- Kinetics of conformation change of sperm-whale myoglobin. I. Folding and unfolding of metmyoglobin following pH jumpBiochemistry, 1972
- Kinetics of conformation change of sperm-whale myoglobin. III. Folding and unfolding of apomyoglobin and the suggested overall mechanismBiochemistry, 1972
- β-Galactosidase: Immunological Activity of Ribosome-Bound, Growing Polypeptide ChainsProceedings of the National Academy of Sciences, 1972