Design of Proteins with Specified Thermal Properties

Дата и время публикации : 1996-01-25T08:46:47Z

Авторы публикации и институты :
Michael P. Morrissey (Harvard University)
Eugene I. Shakhnovich (Harvard University)

Ссылка на журнал-издание: Ссылка на журнал-издание не найдена
Коментарии к cтатье: 12 pages (RevTeX) + 4 postscript figures
Первичная категория: cond-mat

Все категории : cond-mat, q-bio

Краткий обзор статьи: We propose a new and effective means for designing stable and fast-folding polypeptide sequences using a cumulant expansion of the molecular partition function. This method is unique in that $T_{Z}$, the “cumulant design temperature” entered as a parameter in the design process, is predicted also to be the optimal folding temperature. The method was tested using monte-carlo folding simulations of the designed sequences, at various folding temperatures $T_{F}$. (Folding simulations were run on a cubic lattice for computational convenience, but the design process itself is lattice-independent.) Simulations confirmed that, over a wide range of $T_{Z}$, all designed sequences folded rapidly when $T_{F} approx T_{Z}$. Additionally, highly thermostable model proteins were created simply by designing with high $T_{Z}$. The mechanism proposed in these studies provides a plausible pathway for the evolutionary design of biologically active proteins, which {em must} fold and remain stable within a relatively narrow range of temperatures.

Category: Physics