title: Reduced spectral density mapping of a partially folded fragment of E. coli thioredoxin.
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.
authors.affiliation: 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.edu
authors.forename: Gary W
authors.initials: GW
authors.lastname: Daughdrill
authors.forename: Pamela D
authors.initials: PD
authors.lastname: Vise
authors.forename: Hongjun
authors.initials: H
authors.lastname: Zhou
authors.forename: Xiaomin
authors.initials: X
authors.lastname: Yang
authors.forename: Wen-Feng
authors.initials: WF
authors.lastname: Yu
authors.forename: Maria Luisa
authors.initials: ML
authors.lastname: Tasayco
authors.forename: David F
authors.initials: DF
authors.lastname: Lowry
mesh_terms: D003627:Data Interpretation, Statistical; D004926:Escherichia coli / Q000737:chemistry*; D009682:Magnetic Resonance Spectroscopy; D010455:Peptides / Q000737:chemistry* / Q000302:isolation & purification; D013879:Thioredoxins / Q000737:chemistry* / Q000302:isolation & purification
chemical_list: D010455:Peptides; D013879:Thioredoxins