Published January 1, 2013
| Version v1
Journal article
Open
Spatial ranges of driving forces are a key determinant of protein folding cooperativity and rate diversity
Creators
- 1. Gaziantep Univ, Fac Med, Dept Biophys, TR-27310 Gaziantep, Turkey
- 2. Ataturk Univ, Fac Sci, Dept Phys, TR-25240 Erzurum, Turkey
Description
The physical basis of two-state-like folding transitions and the tremendous diversity in folding rates is elucidated by directly simulating the folding kinetics of 52 representative proteins. Relative to the results from a common modeling approach, the diversity of the simulated folding rates can be increased from similar to 10(2.1) to the experimental similar to 10(6.0) by a modest decrease in the spatial range of the attractive potential. The required theoretical range is consistent with desolvation physics and is notably much more permissive than that needed for two-state-like homopolymer collapse.
Files
bib-5f373966-9a96-4669-a686-029703ce4369.txt
Files
(175 Bytes)
| Name | Size | Download all |
|---|---|---|
|
md5:5a041c079a2874df232a2dc3e957373d
|
175 Bytes | Preview Download |