Journal article
Thermodynamics of cyclophilin catalyzed peptidyl-prolyl isomerization by nmr spectroscopy
Biopolymers, Vol.34(2), pp.171-175
02/1994
DOI: 10.1002/bip.360340203
PMID: 8142586
Abstract
One‐dimensional nmr exchange spectroscopy was carried out to determine thermodynamic parameters of cyclophilin‐induced cis‐trans isomerization of succinyl‐Ala‐Phe‐Pro‐Phe‐p‐nitroanilide. Rate measurements were possible at physiological temperatures. The kc/Km of rat cyclophilin was found to he 12.8 (±0.5) s−1 μM−1 at 37°C, intermediate to previously reported values that used a coupled enzyme assay extrapolated to this temperature. Activation energies (ΔG≠) for the uncatalyzed and catalyzed reaction at 37°C were found to be 19.7 and 17.1 kcal/mol, respectively, and were primarily due to an enthalpic barrier. © 1994 John Wiley & Sons, Inc. Copyright © 1994 John Wiley & Sons, Inc.
Details
- Title: Subtitle
- Thermodynamics of cyclophilin catalyzed peptidyl-prolyl isomerization by nmr spectroscopy
- Creators
- John S. Videen - University of California, San DiegoMark A. Stamnes - University of California, San DiegoVictor L. Hsu - University of California, San DiegoMurray Goodman - University of California, San Diego
- Resource Type
- Journal article
- Publication Details
- Biopolymers, Vol.34(2), pp.171-175
- Publisher
- Wiley Subscription Services, Inc., A Wiley Company
- DOI
- 10.1002/bip.360340203
- PMID
- 8142586
- ISSN
- 0006-3525
- eISSN
- 1097-0282
- Number of pages
- 5
- Language
- English
- Date published
- 02/1994
- Academic Unit
- Molecular Physiology and Biophysics; Internal Medicine
- Record Identifier
- 9984297500602771
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