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FlgM gains structure in living cells.


ABSTRACT: 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 results provide insight into how the environment of intrinsically disordered proteins could dictate their structure and, in turn, emphasize the relevance of studying proteins in living cells and in vitro under physiologically realistic conditions.

SUBMITTER: Dedmon MM 

PROVIDER: S-EPMC130520 | biostudies-literature | 2002 Oct

REPOSITORIES: biostudies-literature

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FlgM gains structure in living cells.

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]

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