Thermodynamically Important Contacts in Folding of Model Proteins

Дата и время публикации : 2000-12-15T14:53:26Z

Авторы публикации и институты :
Antonio Scala
Nikolay V. Dokholyan
Sergey V. Buldyrev
H. Eugene Stanley

Ссылка на журнал-издание: Ссылка на журнал-издание не найдена
Коментарии к cтатье: 5 pages, 5 figures; to be published in PRE
Первичная категория: cond-mat.stat-mech

Все категории : cond-mat.stat-mech, q-bio

Краткий обзор статьи: We introduce a quantity, the entropic susceptibility, that measures the thermodynamic importance-for the folding transition-of the contacts between amino acids in model proteins. Using this quantity, we find that only one equilibrium run of a computer simulation of a model protein is sufficient to select a subset of contacts that give rise to the peak in the specific heat observed at the folding transition. To illustrate the method, we identify thermodynamically important contacts in a model 46-mer. We show that only about 50% of all contacts present in the protein native state are responsible for the sharp peak in the specific heat at the folding transition temperature, while the remaining 50% of contacts do not affect the specific heat.

Category: Physics