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Science 20 March 1998:
Vol. 279. no. 5358, pp. 1925 - 1929
DOI: 10.1126/science.279.5358.1925
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Reports

Docking Phospholipase A2 on Membranes Using Electrostatic Potential-Modulated Spin Relaxation Magnetic Resonance

Ying Lin, Robert Nielsen, Diana Murray, Wayne L. Hubbell, Colin Mailer, Bruce H. Robinson, * Michael H. Gelb *

A method involving electron paramagnetic resonance spectroscopy of a site-selectively spin-labeled peripheral membrane protein in the presence and absence of membranes and of a water-soluble spin relaxant (chromium oxalate) has been developed to determine how bee venom phospholipase A2 sits on the membrane. Theory based on the Poisson-Boltzmann equation shows that the rate of spin relaxation of a protein-bound nitroxide by a membrane-impermeant spin relaxant depends on the distance (up to tens of angstroms) from the spin probe to the membrane. The measurements define the interfacial binding surface of this secreted phospholipase A2.

Y. Lin and M. H. Gelb, Department of Chemistry and Department of Biochemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA.
R. Nielsen, C. Mailer, B. H. Robinson, Department of Chemistry, University of Washington, Box 351700, Seattle, WA 98195-1700, USA.
D. Murray, Department of Physiology, State University of New York at Stony Brook, Health Science Center, Stony Brook, NY, 11794-8661, USA.
W. L. Hubbell, Jules Stein Eye Institute, Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024-7008, USA.
*   To whom correspondence should be addressed. E-mail: robinson{at}chem.washington.edu (B.H.R.) and gelb{at}chem.washington.edu (M.H.G.).

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