期刊
PROTEIN SCIENCE
卷 18, 期 4, 页码 811-824出版社
WILEY
DOI: 10.1002/pro.89
关键词
chemical exchange; cyclophilin-A; dynamics; peptidyl-prolyl isomerase; relaxation; nuclear magnetic resonances; enzymes; NMR spectroscopy
资金
- National Science Foundation [MC8B0820567]
- National High Magnetic Field Laboratory (NHMFL)
- State of Florida
- Departments of Molecular & Medical Genetics Biochemistry
- University of Toronto, Ontario, Canada
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0820567] Funding Source: National Science Foundation
With the recent advances in NMR relaxation techniques, protein motions on functionally important timescales can be studied at atomic resolution. Here, we have used NMR-based relaxation experiments at several temperatures and both 600 and 900 MHz to characterize the inherent dynamics of the enzyme cyclophilin-A (CypA). We have discovered multiple chemical exchange processes within the enzyme that form a dynamic continuum'' that spans 20-30 angstrom comprising active site residues and residues proximal to the active site. By combining mutagenesis with these NMR relaxation techniques, a simple method of counting the dynamically sampled conformations has been developed. Surprisingly, a combination of point mutations has allowed for the specific regulation of many of the exchange processes that occur within CypA, suggesting that the dynamics of an enzyme may be engineered.
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