An NMR view of the folding process of a CheY mutant at the residue level.
An NMR view of the folding process of a CheY mutant at the residue level.
Related Articles An NMR view of the folding process of a CheY mutant at the residue level. Structure. 2002 Sep;10(9):1173-1185 Authors: Garcia P, Serrano L, Rico M, Bruix M The folding of CheY mutant F14N/V83T was studied at 75 residues by NMR. Fluorescence, NMR, and sedimentation equilibrium studies at different urea and protein concentrations reveal that the urea-induced unfolding of this CheY mutant includes an on-pathway molten globule-like intermediate that can associate off-pathway. The populations of native and denatured forms have been quantified from a series of 15N-1H HSQC spectra recorded under increasing concentrations of urea. A thermodynamic analysis of these data provides a detailed picture of the mutant's unfolding at the residue level: (1) the transition from the native state to the molten globule-like intermediate is highly cooperative, and (2) the unfolding of this state is sequential and yields another intermediate showing a collapsed N-terminal domain and an unfolded C-terminal tail. This state presents a striking similarity to the kinetic transition state of the CheY folding pathway. PMID: 12220489 [PubMed - indexed for MEDLINE] Source: PubMed |
All times are GMT. The time now is 04:44 PM. |
Powered by vBulletin® Version 3.7.3
Copyright ©2000 - 2024, Jelsoft Enterprises Ltd.
Search Engine Friendly URLs by vBSEO 3.6.0
Copyright, BioNMR.com, 2003-2013