Journal article
Reduced spectral density mapping of a partially folded fragment of E. coli thioredoxin
Journal of biomolecular structure & dynamics, Vol.21(5), pp.663-670
04/2004
Handle:
https://hdl.handle.net/2376/115417
PMID: 14769059
Abstract
The backbone dynamics of a partially folded, N-terminal fragment of E. coli thioredoxin were investigated using nuclear magnetic resonance spectroscopy (NMR). Relaxation data were collected at three temperatures and analyzed using reduced spectral density mapping. As temperature was increased, the values for the viscosity normalized J(0) and for J(omegaH) increased, while J(omegaN) decreased. The global trend observed for the viscosity normalized J(0) was consistent with an increase in the hydrodynamic volume of the fragment and suggested the presence of correlated rotational motion in the absence of long range interactions. In addition, the residue specific variation observed for the viscosity normalized J(0) suggested contributions to J(omega) from a range of correlation times that are close to the global correlation time.
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Details
- Title
- Reduced spectral density mapping of a partially folded fragment of E. coli thioredoxin
- Creators
- Gary W Daughdrill - Department of Microbiology, Molecular Biology and Biochemistry, University of Idaho, PO Box 443052, Life Science South Rm 142, Moscow, ID 83844-3052, USA. gdaugh@uidaho.eduPamela D ViseHongjun ZhouXiaomin YangWen-Feng YuMaria Luisa TasaycoDavid F Lowry
- Publication Details
- Journal of biomolecular structure & dynamics, Vol.21(5), pp.663-670
- Academic Unit
- Engineering and Applied Sciences (TRIC), School of
- Publisher
- England
- Identifiers
- 99900548278001842
- Language
- English
- Resource Type
- Journal article