Ontology highlight
ABSTRACT:
SUBMITTER: Hanson JA
PROVIDER: S-EPMC2084295 | biostudies-literature | 2007 Nov
REPOSITORIES: biostudies-literature
Hanson Jeffrey A JA Duderstadt Karl K Watkins Lucas P LP Bhattacharyya Sucharita S Brokaw Jason J Chu Jhih-Wei JW Yang Haw H
Proceedings of the National Academy of Sciences of the United States of America 20071107 46
Many enzymes mold their structures to enclose substrates in their active sites such that conformational remodeling may be required during each catalytic cycle. In adenylate kinase (AK), this involves a large-amplitude rearrangement of the enzyme's lid domain. Using our method of high-resolution single-molecule FRET, we directly followed AK's domain movements on its catalytic time scale. To quantitatively measure the enzyme's entire conformational distribution, we have applied maximum entropy-bas ...[more]