NDLI: Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.

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Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.

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Backbone and side-chain heteronuclear resonance assignments and hyperfine NMR shifts in horse cytochrome c.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Wand, A. Joshua Rumbley, Jon Englander, S. Walter Liu, Weixia
Description	Country affiliation: United States Author Affiliation: Liu W ( Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA.)
Abstract	The [H26N, H33N] mutant of horse heart cytochrome c was expressed in E. coli during growth on isotopically enriched minimal media. Complete resonance assignments of both the diamagnetic reduced (spin zero) and paramagnetic oxidized (spin (1/2)) states of the protein were obtained using standard triple resonance and total correlation spectroscopy using the previously determined (1)H chemical shifts of the wild-type protein as a guide. The correspondence of chemical shifts between the wild type and the mutant protein is excellent, indicating that they have nearly identical structures. The expanded library of chemical shifts for both redox states in both proteins allowed the refinement of the electron spin g-tensor of the oxidized states. The g-tensors of the oxidized states of the wild-type and [H26N, H33N] mutant proteins are closely similar, indicating that the subtle details of the ligand fields are nearly identical. The refined g-tensors were then used to probe for redox-dependent structure change in the two proteins.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	12
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2003-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cytochromes c Chemistry Animals Electron Spin Resonance Spectroscopy Escherichia Coli Metabolism Heme Horses Magnetic Resonance Spectroscopy Oxidation-reduction Research Support, U.s. Gov't, P.h.s. Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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