Journal article
Defining Protein Ensembles with Native-state NH Exchange: Kinetics of Interconversion and Cooperative Units from Combined NMR and MS Analysis
Journal of molecular biology, Vol.285(3), pp.1265-1275
01/22/1999
DOI: 10.1006/jmbi.1998.2338
PMID: 9887275
Abstract
Previous studies of native-state peptide hydrogen atom (NH) exchange in turkey ovomucoid third domain (OMTKY3) yielded the thermodynamics and kinetics of unfolding and folding for the 14 slowest-exchanging peptide hydrogen atoms (NHs). Unfolding rate constants and free energies for nine of the NHs are very similar, suggesting that these NHs exchange during a single cooperative unfolding event. Electrospray ionization mass spectrometry (ESI-MS) has been used to test this hypothesis. ESI-MS data and MS peak simulations suggest that this hypothesis is incorrect: in spite of the similarity in their unfolding rate constants, only three to five of the nine residues exchange in a cooperative manner. Thus, residues with similar thermodynamics and kinetics of exchange are probably involved in multiple conformational equilibria. Overall, combined NMR and MS analysis of NH exchange provides a rich and complex picture of the ensemble properties of native proteins.
Details
- Title: Subtitle
- Defining Protein Ensembles with Native-state NH Exchange: Kinetics of Interconversion and Cooperative Units from Combined NMR and MS Analysis
- Creators
- Cammon B. Arrington - National Student Clearinghouse Research CenterLynn M. Teesch - University of IowaAndrew D. Robertson - University of Iowa
- Resource Type
- Journal article
- Publication Details
- Journal of molecular biology, Vol.285(3), pp.1265-1275
- Publisher
- Elsevier Ltd
- DOI
- 10.1006/jmbi.1998.2338
- PMID
- 9887275
- ISSN
- 0022-2836
- eISSN
- 1089-8638
- Language
- English
- Date published
- 01/22/1999
- Academic Unit
- Core Research Facilities; Medicine Administration
- Record Identifier
- 9984622756802771
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