Ontology highlight
ABSTRACT:
SUBMITTER: Dedmon MM
PROVIDER: S-EPMC130520 | biostudies-literature | 2002 Oct
REPOSITORIES: biostudies-literature
Dedmon Matthew M MM Patel Chetan N CN Young Gregory B GB Pielak Gary J GJ
Proceedings of the National Academy of Sciences of the United States of America 20020923 20
Intrinsically disordered proteins such as FlgM play important roles in biology, but little is known about their structure in cells. We use NMR to show that FlgM gains structure inside living Escherichia coli cells and under physiologically relevant conditions in vitro, i.e., in solutions containing high concentrations (>/=400 g/liter) of glucose, BSA, or ovalbumin. Structure formation represents solute-induced changes in the equilibrium between the structured and disordered forms of FlgM. The re ...[more]