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.
journal_name
Proc Natl Acad Sci U S Aauthors
Oldfield E,Gilmore R,Glaser M,Gutowsky HS,Hshung JC,Kang SY,King TE,Meadows M,Rice Ddoi
10.1073/pnas.75.10.4657subject
Has Abstractpub_date
1978-10-01 00:00:00pages
4657-60issue
10eissn
0027-8424issn
1091-6490journal_volume
75pub_type
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