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Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin

Koenig, B. W. and Mitchell, D. C. and Konig, S. and Grzesiek, S. and Litman, B. J. and Bax, A.. (2000) Measurement of dipolar couplings in a transducin peptide fragment weakly bound to oriented photo-activated rhodopsin. Journal of Biomolecular NMR, 16 (2). pp. 121-125.

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Official URL: http://edoc.unibas.ch/dok/A5258805

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Abstract

Rhodopsin-containing disks, isolated from rod outer segments of bovine retina, align at high magnetic fields with their membrane normal parallel to the magnetic field. After light-activation of rhodopsin, transient binding of the C-terminal transducin undecapeptide, selectively labeled with 15N at Leu5 and Gly9, results in residual dipolar contributions to the 1J(NH) splittings for these two residues. Both residues show 1J(NH) splittings which are smaller than in the dark- adapted or rhodopsin-free sample, and return to their isotropic values at a rate determined by the decay of the meta II state of rhodopsin. The dipolar couplings indicate that in the bound state, N-H vectors of Leu5 and Gly9 make angles of 48+/-4 degrees and 40+/-8 degrees, respectively, with the disk normal. These 'transferred' dipolar couplings potentially offer a useful method for studying the conformation and orientation of flexible, low affinity ligands when bound to oriented integral membrane receptors.
Faculties and Departments:05 Faculty of Science > Departement Biozentrum > Structural Biology & Biophysics > Structural Biology (Grzesiek)
UniBasel Contributors:Grzesiek, Stephan
Item Type:Article, refereed
Article Subtype:Research Article
Bibsysno:Link to catalogue
Publisher:Springer
ISSN:0925-2738
e-ISSN:1573-5001
Note:Publication type according to Uni Basel Research Database: Journal article
Language:English
Identification Number:
Last Modified:23 Nov 2017 11:27
Deposited On:22 Mar 2012 13:21

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