sup 2 H Nuclear magnetic resonance of the gramicidin A backbone in a phospholipid bilayer
- Univ. of Guelph, Ontario (Canada)
- Univ. of Oregon, Eugene (USA)
Solid-state {sup 2}H NMR spectroscopy has been employed to study the channel conformation of gramicidin A (GA) in unoriented 1,2-dimyristoyl-sn-glycerol-3-phosphocholine (DMPC) multilayers. Quadrupolar echo spectra were obtained at 44{degree}C and 53{degree}C, from gramicidin A labels in which the proton attached to the {alpha} carbon of residue 3,4,5,10,12, or 14 was replaced with deuterium. Because of the nearly axially symmetric electric field gradient tensor, the quadrupolar splittings obtained from an unoriented multilamellar dispersion of DMPC and singly labeled GA directly yield unambiguous orientational constraints on the C-{sup 2}H bonds. The authors conclude that the helix sense of the channel conformation of GA is right-handed. Assuming that the dominant motions are fast axial diffusion of the gramicidin molecule and reorientation of the diffusion axis with respect to the local bilayer normal, then the theoretical splittings may all be scaled down by a constant motional narrowing factor.
- OSTI ID:
- 5596630
- Journal Information:
- Biochemistry; (United States), Journal Name: Biochemistry; (United States) Vol. 30:19; ISSN 0006-2960; ISSN BICHA
- Country of Publication:
- United States
- Language:
- English
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Related Subjects
59 BASIC BIOLOGICAL SCIENCES
ALANINES
ALCOHOLS
AMINES
AMINO ACIDS
AMMONIUM COMPOUNDS
CARBOXYLIC ACIDS
CHOLINE
DEUTERIUM COMPOUNDS
DICHROISM
DRUGS
ESTERS
HYDROGEN COMPOUNDS
HYDROXY COMPOUNDS
LEUCINE
LIPIDS
LIPOTROPIC FACTORS
MAGNETIC CIRCULAR DICHROISM
MAGNETIC RESONANCE
MEMBRANE PROTEINS
MEMBRANES
MOLECULAR STRUCTURE
NUCLEAR MAGNETIC RESONANCE
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PEPTIDES
PHOSPHOLIPIDS
PROTEINS
QUATERNARY COMPOUNDS
RESONANCE