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National Institute of Environmental Health Sciences

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Publication Detail

Title: Docking phospholipase A2 on membranes using electrostatic potential-modulated spin relaxation magnetic resonance.

Authors: Lin, Y; Nielsen, R; Murray, D; Hubbell, W L; Mailer, C; Robinson, B H; Gelb, M H

Published In Science, (1998 Mar 20)

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 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.

PubMed ID: 9506941 Exiting the NIEHS site

MeSH Terms: No MeSH terms associated with this publication

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