Book chapter
Measuring the conformational stability of a protein by hydrogen exchange
Protein Structure, Stability, and Folding, pp.69-92
Methods in molecular biology (Clifton, N.J.), v. 168, Humana Press
2001
DOI: 10.1385/1-59259-193-0:069
PMID: 11357629
Abstract
Measuring the conformational stability of a protein is one key to solving the protein folding problem. It is also of practical importance for answering questions such as these:
1. How stable is a protein under physiological conditions?
2. How does the stability depend on temperature, pH, and salt concentration?
3. Can the stability be increased by osmolytes?
4. Can the stability be increased by ligands that bind the native state?
5. Does an amino-acid substitution increase or decrease the stability?
Thus, reliable techniques for measuring the conformational stability of proteins are essential. In this chapter, we briefly review the traditional methods that have been used to measure the conformational stability of a protein, and describe in more detail how the conformational stability can be measured using hydrogen-exchange rates as monitored by nuclear magnetic resonance (NMR).
Details
- Title: Subtitle
- Measuring the conformational stability of a protein by hydrogen exchange
- Creators
- Beatrice M. P. Huyghues‐DespointesC. Nick PaceS. Walter EnglanderJ. Martin Scholtz
- Resource Type
- Book chapter
- Publication Details
- Protein Structure, Stability, and Folding, pp.69-92
- Publisher
- Humana Press; Totowa, New Jersey
- Series
- Methods in molecular biology (Clifton, N.J.); v. 168
- DOI
- 10.1385/1-59259-193-0:069
- PMID
- 11357629
- ISSN
- 1064-3745
- eISSN
- 1940-6029
- Language
- English
- Date published
- 2001
- Academic Unit
- Research Administration; Pharmaceutical Sciences and Experimental Therapeutics; Biochemistry and Molecular Biology; Chemistry
- Record Identifier
- 9984288727802771
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