Correlated motions in native proteins from MS analysis of NH exchange: evidence for a manifold of unfolding reactions in ovomucoid third domain
- 30 June 2000
- journal article
- Published by Elsevier in Journal of Molecular Biology
- Vol. 300 (1) , 221-232
- https://doi.org/10.1006/jmbi.2000.3859
Abstract
No abstract availableKeywords
This publication has 44 references indexed in Scilit:
- The atomic structure of protein-protein recognition sites 1 1Edited by A. R. FershtJournal of Molecular Biology, 1999
- Defining Protein Ensembles with Native-state NH Exchange: Kinetics of Interconversion and Cooperative Units from Combined NMR and MS AnalysisJournal of Molecular Biology, 1999
- Molten Globule Unfolding Monitored by Hydrogen Exchange in UreaBiochemistry, 1998
- Hydrogen exchange properties of proteins in native and denatured states monitored by mass spectrometry and NMRProtein Science, 1997
- Protein Folding Intermediates: Native-State Hydrogen ExchangeScience, 1995
- Funnels, pathways, and the energy landscape of protein folding: A synthesisProteins-Structure Function and Bioinformatics, 1995
- Primary structure effects on peptide group hydrogen exchangeProteins-Structure Function and Bioinformatics, 1993
- Ligand binding to heme proteins: relevance of low-temperature dataBiochemistry, 1986
- The crystal and molecular structure of the third domain of silver pheasant ovomucoid (OMSVP3)European Journal of Biochemistry, 1985
- Thermodynamic fluctuations in protein molecules.Proceedings of the National Academy of Sciences, 1976