Ontology highlight
ABSTRACT:
SUBMITTER: Saio T
PROVIDER: S-EPMC4652230 | biostudies-literature | 2015 Nov
REPOSITORIES: biostudies-literature
Scientific reports 20151119
Proteins, especially multi-domain proteins, often undergo drastic conformational changes upon binding to ligands or by post-translational modifications, which is a key step to regulate their function. However, the detailed mechanisms of such dynamic regulation of the functional processes are poorly understood because of the lack of an efficient tool. We here demonstrate detailed characterization of conformational changes of MurD, a 47 kDa protein enzyme consisting of three domains, by the use of ...[more]