Probing the folding intermediate of Bacillus subtilis RNase P protein by nuclear magnetic resonance

Authors :: Yu-Chu Chang
Franch, William R.
Oas, Terrence G.
Source :: Biochemistry. Nov 9, 2010, Vol. 49 Issue 44, 9428-9437
Publication Year :: 2010
Abstract: The nuclear magnetic resonance spectroscopy technique is employed to identify the folding intermediate associated with the Bacillus subtilis RNase P protein. The results demonstrate the presence of an equilibrium, as well as kinetic intermediate in the folding mechanism of the protein.

Subjects :: Bacillus subtilis -- Physiological aspects
Nuclear magnetic resonance spectroscopy -- Usage
Protein folding -- Analysis
Ribonuclease -- Structure
Ribonuclease -- Chemical properties
Biological sciences
Chemistry

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