Ontology highlight
ABSTRACT:
SUBMITTER: Smith AE
PROVIDER: S-EPMC4420520 | biostudies-literature | 2015 May
REPOSITORIES: biostudies-literature
Smith Austin E AE Zhou Larry Z LZ Pielak Gary J GJ
Protein science : a publication of the Protein Society 20150302 5
A truly disordered protein lacks a stable fold and its backbone amide protons exchange with solvent at rates predicted from studies of unstructured peptides. We have measured the exchange rates of two model disordered proteins, FlgM and α-synuclein, in buffer and in Escherichia coli using the NMR experiment, SOLEXSY. The rates are similar in buffer and cells and are close to the rates predicted from data on small, unstructured peptides. This result indicates that true disorder can persist inside ...[more]