Rate determining factors in protein model structures.
Previous research has shown a strong correlation of protein folding rates to the native state geometry, yet a complete explanation for this dependence is still lacking. Here we study the rate-geometry relationship with a simple statistical physics model, and focus on two classes of model geometries, representing ideal parallel and antiparallel structures. We find that the logarithm of the rate shows an almost perfect linear correlation with the "absolute contact order", but the slope depends on the particular class considered. We discuss these findings in the light of experimental results.
Bruscolini
Pierpaolo
P
Instituto de Biocomputación y Física de Sistemas Complejos (BIFI), Universidad de Zaragoza, c. Corona de Aragón 42, 50009 Zaragoza, Spain. pier@unizar.es
Pelizzola
Alessandro
A
Zamparo
Marco
M
D015233:Models, Statistical; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013816:Thermodynamics
D011506:Proteins