## Abstract The diffusion–collision model (DCM) of protein folding is described qualitatively and quantitatively. The input parameters required to perform a calculation are explained, and the output data are outlined. Three examples are given of calculating DCM folding kinetics: the Engrailed Homeo
Diffusion–collision model for protein folding
✍ Scribed by Martin Karplus; David L. Weaver
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1979
- Tongue
- English
- Weight
- 823 KB
- Volume
- 18
- Category
- Article
- ISSN
- 0006-3525
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✦ Synopsis
Abstract
The basic equations for the elementary step in the diffusion–collision–coalescence model of protein folding are derived for the case of two radially diffusing spherical microdomains. Refinements and biological implications of the mechanism are considered; included are detailed discussions of the parameters of the model, the possibilities of rotational diffusion and surface diffusion in one or two dimensions, the nature of the microdomains, and the application of the model to protein unfolding.
📜 SIMILAR VOLUMES
The diffusion-collision model of protein folding has been solved exactly for a three-microdomain protein subunit. Numerical analysis shows that the exact kinetics may be excellently approximated in all cases studied by a standard chemical kinetics approach with the forward rate constants calculated
## 4 It('[['r<)[){]l!fn ('r tnodel (d rundoml~.scll~in(eruc[itrgchuirrs /n [MOdimcn.sitms is .studicd Lt'i[h numericul ,sitnulu(ions {n order [C] ehicida(e th(~.ji]ldingmechanism oj protein. H),find (hat the model occasionally . SIMN{ .S,li~lding propen.si[~,depending on [he .wqacnce ()/" random nam
We outline a general strategy for determining the effective coarse-grained interactions between the amino acids of a protein from the experimentally derived nativestate structures. The method is, in principle, free from any adjustable or empirically determined parameters, and it is tested on simple
Chaperonins are oligomeric proteins that help other proteins fold. They act, according to the "Anfinsen cage" or "box of infinite dilution" model, to provide private space, protected from aggregation, where a protein can fold. Recent evidence indicates, however, that proteins are often ejected from