1. Molten globule unfolding monitored by hydrogen exchange in urea
- Author
-
Chamberlain, Aaron K. and Marqusee, Susan
- Subjects
Escherichia coli -- Genetic aspects ,Ion exchange -- Usage ,Proteins -- Denaturation ,Ribonuclease -- Analysis ,Biological sciences ,Chemistry - Abstract
A research was conducted to examine how the energetics of individual regions react to the presence of denaturant in the molten globule condition of Escherichia coli ribonuclease H1. Quenched hydrogen exchange reactions and nuclear magnetic resonance sample preparation were utilized at 4 degrees C. Protonated solutions were also used to evaluate which protons could serve as probes of the molten globule structure. Results showed that the free energy of hydrogen exchange declined linearly with increases in denaturant concentrations.
- Published
- 1998