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Published online before print December 20, 2007, 10.1110/ps.073174008
Protein Science (2008), 17:228-239. Published by Cold Spring Harbor Laboratory Press. Copyright © 2008 The Protein Society
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Structural determinants of nitroxide motion in spin-labeled proteins: Solvent-exposed sites in helix B of T4 lysozyme

Zhefeng Guo1,4, Duilio Cascio2, Kálmán Hideg3, and Wayne L. Hubbell1

1 Jules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California, Los Angeles, California 90095-7008, USA
2 UCLA-DOE Institute for Genomics and Proteomics, University of California, Los Angeles, California 90095-1570, USA
3 Institute of Organic and Medical Chemistry, University of Pécs, H-7643 Pécs, Hungary

(RECEIVED August 20, 2007; FINAL REVISION October 24, 2007; ACCEPTED October 31, 2007)

Site-directed spin labeling provides a means for exploring structure and dynamics in proteins. To interpret the complex EPR spectra that often arise, it is necessary to characterize the rotamers of the spin-labeled side chain and the interactions they make with the local environment in proteins of known structure. For this purpose, crystal structures have been determined for T4 lysozyme bearing a nitroxide side chain (R1) at the solvent-exposed helical sites 41 and 44 in the B helix. These sites are of particular interest in that the corresponding EPR spectra reveal two dynamic states of R1, one of which is relatively immobilized suggesting interactions of the nitroxide with the environment. The crystal structures together with the effect of mutagenesis of nearest neighbors on the motion of R1 suggest intrahelical interactions of 41R1 with the i + 4 residue and of 44R1 with the i + 1 residue. Such interactions appear to be specific to particular rotamers of the R1 side chain.

Keywords: site-directed spin labeling; EPR spectroscopy; side-chain conformation


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