Ontology highlight
ABSTRACT:
SUBMITTER: Chakraborty D
PROVIDER: S-EPMC5241393 | biostudies-literature | 2015 Oct
REPOSITORIES: biostudies-literature
The journal of physical chemistry. B 20150923 40
We present a systematic computational investigation of the internal hydration of a set of homologous proteins of different stability content and molecular complexities. The goal of the study is to verify whether structural water can be part of the molecular mechanisms ensuring enhanced stability in thermophilic enzymes. Our free-energy calculations show that internal hydration in the thermophilic variants is generally more favorable, and that the cumulated effect of wetting multiple sites result ...[more]