Journal
PROTEIN SCIENCE
Volume 18, Issue 4, Pages 811-824Publisher
WILEY
DOI: 10.1002/pro.89
Keywords
chemical exchange; cyclophilin-A; dynamics; peptidyl-prolyl isomerase; relaxation; nuclear magnetic resonances; enzymes; NMR spectroscopy
Categories
Funding
- 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
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available