학술논문
Globally correlated conformational entropy underlies positive and negative cooperativity in a kinase’s enzymatic cycle
Document Type
article
Author
Source
Nature Communications, Vol 10, Iss 1, Pp 1-11 (2019)
Subject
Language
English
ISSN
2041-1723
Abstract
Allosteric interactions are an important contributor to the catalytic properties of enzyme. Here the authors demonstrate—using the prototypical protein kinase PKA—that the allosteric cooperativity underscoring substrate recognition and product release are directly linked to changes in conformational entropy.