Title | Characterization of folding the four-helix bundle protein Rop by real-time NMR. |
Publication Type | Journal Article |
Year of Publication | 2008 |
Authors | van Nuland, N. A. J., C. M. Dobson, and L. Regan |
Journal | Protein Eng Des Sel |
Volume | 21 |
Issue | 3 |
Pagination | 165-70 |
Date Published | 2008 Mar |
ISSN | 1741-0126 |
Keywords | Bacterial 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. |
DOI | 10.1093/protein/gzm081 |
Alternate Journal | Protein Eng. Des. Sel. |
PubMed ID | 18299292 |
Grant List | GM49146-01A1 / 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 |
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