Spin-label Electron Spin Resonance Study of Bacteriophage M13 Coat Protein Incorporation into Mixed Lipid Bilayers

Overview

Journal Biochemistry

Specialty Biochemistry

Date 1987 Dec 1

PMID 2827755

Citations 6

Authors

K P Datema

C J Wolfs

D Marsh

A Watts

M A Hemminga

Affiliations

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Abstract

The major coat protein of bacteriophage M13 was incorporated in mixed dimyristoylphosphatidylcholine/dimyristoylphosphatidylglycerol (80/20 w/w) vesicles probed with different spin-labeled phospholipids, labeled on the C-14 atom of the sn-2 chain. The specificity for a series of phospholipids was determined from a motionally restricted component seen in the electron spin resonance (ESR) spectra of vesicles with the coat protein incorporated. At 30 degrees C and pH 8, the fraction of motionally restricted phosphatidic acid spin-label is 0.36, 0.52, and 0.72 for lipid/protein ratios of 18, 14, and 9 mol/mol, respectively. The ESR spectra, analyzed by digital subtraction, resulted in a phospholipid preference following the pattern cardiolipin = phosphatidic acid greater than stearic acid = phosphatidylserine = phosphatidylglycerol greater than phosphatidylcholine = phosphatidylethanolamine. The specificities found are related to the composition of the target Escherichia coli cytoplasmic membrane.

Citing Articles

Electron spin resonance in membrane research: protein-lipid interactions from challenging beginnings to state of the art.

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Quantification of Protein-Lipid Selectivity using FRET: Application to the M13 Major Coat Protein.

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Analysis of time-resolved fluorescence anisotropy in lipid-protein systems. II. Application to tryptophan fluorescence of bacteriophage M13 coat protein incorporated in phospholipid bilayers.

Peng K, Visser A, van Hoek A, Wolfs C, Hemminga M Eur Biophys J. 1990; 18(5):285-93.

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Analysis of time-resolved fluorescence anisotropy in lipid-protein systems. I. Application to the lipid probe octadecyl rhodamine B in interaction with bacteriophage M13 coat protein incorporated in phospholipid bilayers.

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