FlgM gains structure in living cells
- Departments of *Chemistry, and †Biochemistry and Biophysics, and ‡Lineberger Cancer Research Center, University of North Carolina, Chapel Hill, NC 27599
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Edited by S. Walter Englander, University of Pennsylvania School of Medicine, Swarthmore, PA, and approved August 8, 2002 (received for review June 4, 2002)
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.
Footnotes
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↵ § To whom reprint requests should be addressed. E-mail: gary_pielak{at}unc.edu.
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This paper was submitted directly (Track II) to the PNAS office.
- Abbreviation:
- HSQC,
- heteronuclear single quantum correlation
- Copyright © 2002, The National Academy of Sciences
