Journal article
Measuring the conformational stability of a protein by NMR
CSH protocols, Vol.2006(1), p.pdb.prot4244
06/01/2006
DOI: 10.1101/pdb.prot4244
Abstract
This protocol describes an NMR technique to measure the stability of a protein by hydrogen exchange. When a protein is placed in D2O, amide hydrogens in the protein begin to exchange with deuterium. Unprotected amides exchange readily with the solvent. In contrast, amides that are shielded from solvent by burial and/or hydrogen bonding can exchange only when the local amide region of the protein unfolds to some higher-energy conformation, thus exposing the amide to solvent. The result is that exchange rates of amide protons in a protein vary widely, providing a clear view of the higher-energy unfolded states under native conditions (Chamberlain and Marqusee 1997).
Details
- Title: Subtitle
- Measuring the conformational stability of a protein by NMR
- Creators
- Gerald R GrimsleyBeatrice M P Huyghues-DespointesC Nick PaceJ Martin Scholtz
- Resource Type
- Journal article
- Publication Details
- CSH protocols, Vol.2006(1), p.pdb.prot4244
- DOI
- 10.1101/pdb.prot4244
- ISSN
- 1940-3402
- eISSN
- 1559-6095
- Language
- English
- Date published
- 06/01/2006
- Academic Unit
- Chemistry; Research Administration; Biochemistry and Molecular Biology; Pharmaceutical Sciences and Experimental Therapeutics
- Record Identifier
- 9984293417302771
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