Thermostability of in vitro evolved Bacillus subtilis lipase A: a network and dynamics perspective.

ABSTRACT: Proteins in thermophilic organisms remain stable and function optimally at high temperatures. Owing to their important applicability in many industrial processes, such thermostable proteins have been studied extensively, and several structural factors attributed to their enhanced stability. How these factors render the emergent property of thermostability to proteins, even in situations where no significant changes occur in their three-dimensional structures in comparison to their mesophilic counter-parts, has remained an intriguing question. In this study we treat Lipase A from Bacillus subtilis and its six thermostable mutants in a unified manner and address the problem with a combined complex network-based analysis and molecular dynamic studies to find commonality in their properties. T

SUBMITTER: Srivastava A 

PROVIDER: S-EPMC4133394 | biostudies-literature | 2014

REPOSITORIES: biostudies-literature