Journal article
Determining a urea or guanidinium chloride unfolding curve
CSH protocols, Vol.2006(1), p.pdb.prot4242
06/01/2006
DOI: 10.1101/pdb.prot4242
Abstract
This protocol describes a method for measuring the conformational stability of a protein by determining the equilibrium constant and the free energy change, ΔG, for the reaction Folded (F) ↔ Unfolded (U) using a denaturant. The techniques commonly used to follow protein unfolding are fluorescence, circular dichroism (CD), and UV absorption. The best technique is generally the one that shows the biggest change between the folded and unfolded forms. It is essential that equilibrium is reached before measurements are made and that the unfolding reaction is reversible.
Details
- Title: Subtitle
- Determining a urea or guanidinium chloride unfolding curve
- 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.prot4242
- DOI
- 10.1101/pdb.prot4242
- ISSN
- 1940-3402
- eISSN
- 1559-6095
- Language
- English
- Date published
- 06/01/2006
- Academic Unit
- Pharmaceutical Sciences and Experimental Therapeutics; Chemistry; Research Administration; Biochemistry and Molecular Biology
- Record Identifier
- 9984293559002771
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