Deuterium nuclear magnetic resonance investigation of the effects of proteins and polypeptides on hydrocarbon chain order in model membrane systems.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 75 ·No. 10 ·1978-10-00 ·Pages 4657-60

Oldfield E, Gilmore R, Glaser M, Gutowsky HS, Hshung JC, Kang SY, King TE, Meadows M, Rice D

Abstract

Deuterium Fourier-transform nuclear magnetic resonance spectra have been obtained of 1-myristoyl 2-(14,14,14-trideutero)myristoyl phosphatidylcholine bilayers at 34.1 MHz by using the quadrupole echo pulse technique. Thereby, we have investigated the effects upon the deuterated dimyristoyl phosphatidylcholine bilayers of the following proteins and polypeptides: gramicidin A, bacteriophage f1 coat protein, beef brain myelin proteolipid apoprotein, cytochrome b(5), and cytochrome c oxidase (ferrocytochrome c:oxygen oxidoreductase, EC 1.9.3.1). Above T(c), the transition temperature between the gel and liquid crystal phases, the quadrupole splitting of the deuterium-labeled methyl group is reduced or collapsed in the presence of protein or polypeptide. No evidence has been found for ordered "boundary lipid." Below T(c), the spectra show that the hydrocarbon chains are prevented from crystallizing by the protein (or polypeptide) incorporated in the membrane. Similar disordering effects above T(c) are also seen when an unsaturated lipid, 1-(16,16,16-trideutero)palmitoyl 2-palmitoleyl phosphatidylcholine is complexed with cytochrome oxidase.

Authors & Affiliations

9 authors, click to expand affiliations / ORCID

Oldfield E

School of Chemical Sciences, University of Illinois, Urbana, Illinois 61801.

Gilmore R

Glaser M

Gutowsky H S

Hshung J C

Kang S Y

King T E

Meadows M

Rice D

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23 references, click to expand

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Article Info

Journal

Proceedings of the National Academy of Sciences of the United States of America

Abbr.

Proc Natl Acad Sci U S A

ISSN

0027-8424

DOI

10.1073/pnas.75.10.4657

Published

1978-10-00

Pages

4657-60

Language

English

Region

United States

NLM ID

7505876

PMCID

PMC336175

External Links

PubMed source DOI: 10.1073/pnas.75.10.4657 PMC Full Text View journal details

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Deuterium nuclear magnetic resonance investigation of the effects of proteins and polypeptides on hydrocarbon chain order in model membrane systems.

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