Journal
PROTEIN SCIENCE
Volume 24, Issue 5, Pages 706-713Publisher
WILEY
DOI: 10.1002/pro.2643
Keywords
amide proton exchange; intrinsically disordered proteins; in-cell NMR; SOLEXSY; macromolecular crowding
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Funding
- National Science Foundation [MCB 1051819, MCB 1410854]
- Direct For Biological Sciences
- Div Of Molecular and Cellular Bioscience [1410854] Funding Source: National Science Foundation
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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 -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 the crowded cellular interior and that weak interactions between proteins and macromolecules in cells do not necessarily affect intrinsic rates of exchange.
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