2007/07/18 by Pierpaolo Bruscolini, Alessandro Pelizzola, Marco Zamparo · 1 citation
Biochemistry, Genetics and Molecular Biology · Physics and Astronomy · #Protein Structure and Dynamics #Spectroscopy and Quantum Chemical Studies #Theoretical and Computational Physics #cond-mat.stat-mech #q-bio.BM
paper · pdf · doi:10.1103/physrevlett.99.038103
published as Phys. Rev. Lett. 99, 038103 (2007) · 4 pages, 2 figures
openalex publication_date 2007/07/18 · arxiv created 2007/09/14 · arxiv updated 2009/12/01 · openalex created_date 2025/10/10 · openalex updated_date 2026/08/03
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.