Testing a New Monte Carlo Strategy for Folding Model Proteins
H. Frauenkron, U. Bastolla, E. Gerstner, P. Grassberger, und W. Nadler
Abstract
We demonstrate that the recently proposed pruned-enriched Rosenbluth method PERM (P.~Grassberger, Phys.~Rev.~ E 56 (1997) 3682) leads to very efficient algorithms for the folding of simple model proteins. We test it on several models for lattice heteropolymers, and compare to published Monte Carlo studies of the properties of particular sequences. In all cases our method is faster than the previous ones, and in several cases we find new minimal energy states. In addition to producing more reliable candidates for ground states, our method gives detailed information about the thermal spectrum and, thus, allows to analyze static aspects of the folding behavior of arbitrary sequences.
Create a lesson
Related papers
Charged Three-Dimensional Solitons in a Ferroelectric Nematic Liquid Crystal
Netra Prasad Dhakal, Zakaria Siddiquee, Hiroya Nishikawa et al.
Frank Elastic Constants of Associating Rigid-Rodlike Systems
Akihiko Matsuyama
Medial Model of Elastic Curve Contacts, from Clasps to Knits
Kathryn Chain, Haoye Sun, Michael S. Dimitriyev
How symmetry and complexity shape three-dimensional programmable self-assembly
Prarthana Agrawal, Joakim Bohlin, Ard A. Louis
Designing tunable hyperuniformity in random organization through nonlocal noise
Yusheng Lei, Yuhan Peng, Ran Ni
Long-time Brownian dynamics of hard and sticky colloids by geometric projection
Rémi Martin, Sandrine Duluard, Céline Merlet