Book of Abstracts: Albany 2003

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Abstract Book
June 17-21 2003

An Unfolded Protein that Folds in Living Cells

Intrinsically disordered proteins such as FlgM play important roles in biology, but little is known about their structure in cells. We used 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/L) of glucose, bovine serum albumin, 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. [abstract from Dedmon, M. M., Patel, C. N., Young, G. B., Pielak, G. J. FlgM gains structure in living cells. Proceedings of the National Academy of Sciences of the United States of America 99, 12681-12684 (2002).]

Matthew M. Dedmon1
Chetan N. Patel1
Gregory B. Young2
Gary J. Pielak1,2,*

1Department of Chemistry
2Department of Biochemistry & Biophysics
Lineberger Cancer Research Center
University of North Carolina at Chapel Hill
Chapel Hill, North Carolina 27599