A Criterion That Determines Fast Folding of Proteins: A Model Study

Дата и время публикации : 1996-04-08T19:41:11Z

Авторы публикации и институты :
Carlos J. Camacho (Fisica, PUC, Santiago, Chile)
D. Thirumalai (IPST, U. of Maryland, College Park USA)

Ссылка на журнал-издание: Ссылка на журнал-издание не найдена
Коментарии к cтатье: 10 pages, latex, figures upon request
Первичная категория: chem-ph

Все категории : chem-ph, cond-mat, physics.chem-ph

Краткий обзор статьи: We consider the statistical mechanics of a full set of two-dimensional protein-like heteropolymers, whose thermodynamics is characterized by the coil-to-globular ($T_theta$) and the folding ($T_f$) transition temperatures. For our model, the typical time scale for reaching the unique native conformation is shown to scale as $tau_fsim F(M)exp(sigma/sigma_0)$, where $sigma=1-T_f/T_theta$, $M$ is the number of residues, and $F(M)$ scales algebraically with $M$. We argue that $T_f$ scales linearly with the inverse of entropy of low energy non-native states, whereas $T_theta$ is almost independent of it. As $sigmarightarrow 0$, non-productive intermediates decrease, and the initial rapid collapse of the protein leads to structures resembling the native state. Based solely on {it accessible} information, $sigma$ can be used to predict sequences that fold rapidly.

Category: Physics