Docking Phospholipase A 2 on Membranes Using Electrostatic Potential-Modulated Spin Relaxation Magnetic Resonance-Reference-Cited by-同舟云学术

Docking Phospholipase A 2 on Membranes Using Electrostatic Potential-Modulated Spin Relaxation Magnetic Resonance

Published:1998-03-20 Issue:5358 Volume:279 Page:1925-1929
ISSN:0036-8075
Container-title:Science
language:en
Short-container-title:Science

Author:

Lin Ying¹²³⁴,Nielsen Robert¹²³⁴,Murray Diana¹²³⁴,Hubbell Wayne L.¹²³⁴,Mailer Colin¹²³⁴,Robinson Bruce H.¹²³⁴,Gelb Michael H.¹²³⁴

Affiliation:

1. Y. Lin and M. H. Gelb, Department of Chemistry and Department of Biochemistry, University of Washington, Box 351700, Seattle, WA 98195–1700, USA.

2. R. Nielsen, C. Mailer, B. H. Robinson, Department of Chemistry, University of Washington, Box 351700, Seattle, WA 98195–1700, USA.

3. D. Murray, Department of Physiology, State University of New York at Stony Brook, Health Science Center, Stony Brook, NY, 11794–8661, USA.

4. W. L. Hubbell, Jules Stein Eye Institute, Department of Chemistry and Biochemistry, University of California, Los Angeles, CA 90024–7008, USA.

Abstract

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 A 2 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 A 2 .

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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