Characterization of folding the four-helix bundle protein Rop by real-time NMR.

TitleCharacterization of folding the four-helix bundle protein Rop by real-time NMR.
Publication TypeJournal Article
Year of Publication2008
Authorsvan Nuland, N. A. J., C. M. Dobson, and L. Regan
JournalProtein Eng Des Sel
Volume21
Issue3
Pagination165-70
Date Published2008 Mar
ISSN1741-0126
KeywordsBacterial Proteins, Circular Dichroism, Guanidine, Kinetics, Models, Molecular, Nuclear Magnetic Resonance, Biomolecular, Protein Conformation, Protein Folding, RNA-Binding Proteins
Abstract

Rop is a four-helix bundle protein composed of two identical helix-loop-helix monomers. Protein folding monitored by stopped-flow fluorescence or CD exhibits biphasic kinetics when folding to low final denaturant concentrations. As the final concentration of denaturant is increased, the amplitude of the fast phase decreases, until at the highest concentrations the kinetics appear monophasic. We propose that the fast phase represents the formation of an intermediate. Here, we use real-time NMR to detect the formation of this intermediate and to characterize its structural features.

DOI10.1093/protein/gzm081
Alternate JournalProtein Eng. Des. Sel.
PubMed ID18299292
Grant ListGM49146-01A1 / GM / NIGMS NIH HHS / United States
/ / Biotechnology and Biological Sciences Research Council / United Kingdom
/ / Howard Hughes Medical Institute / United States
/ / Medical Research Council / United Kingdom