Abstract:
:This review article outlines some potentials and limits of the recent application of high resolution Nuclear Magnetic Resonance technique--coupled to the Fourier transformation methods--to the study of biological membranes. Molecular arrangement and dynamical structure characters can be assessed at the level of individual chemical groups in lipid bilayer regions of natural and model membranes, through the determination of physical parameters like chemical shifts, spin-lattice (T1) and spin-spin (T2) nuclear magnetic relaxation times. The results of some significant experiments carried out on single-wall lecithin vesicles as well as on intact natural membranes, are summarized and discussed. Useful information can be obtained on the lipid fatty-acid chains thermal transition, by comparing two lecithin vesicles of the same size, formed by the same host lecithin, but incorporated with different molecular components. In particular, T1 and T2 measurements, interpreted in terms of a two- (or more-) correlation time theoretical models, are able to demonstrate different degrees of motional anisotropy in bilayers formed by mixed lecithins or by mixtures of lecithin and fatty acids, possessing moderately different chain lengths [13]. Chromophore-containing molecules, like chlorophyll [12] or fluorescent probes [14] can be located, within few Angstroms, in a lipid bilayer through proton chemical shift measurements; in addition the perturbation of the lipid membrane structure, as induced by the incorporated probe, is assessed mainly in terms of the intramolecular dynamical structure of the host lecithin molecules, by means of T1 and linewidth studies. The comparison of the n.m.r. relaxation behaviour in intact membranes and in vesicles formed by their extracted lipids may, finally, provide indirect information on the lipid-protein intermolecular interactions and relative mobility, besides indicating the intramolecular mobility characters of the lipid bilayer regions of the membrane.
journal_name
Biochimiejournal_title
Biochimieauthors
Podo Fdoi
10.1016/s0300-9084(75)80333-6keywords:
subject
Has Abstractpub_date
1975-01-01 00:00:00pages
461-9issue
4eissn
0300-9084issn
1638-6183pii
S0300-9084(75)80333-6journal_volume
57pub_type
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