/sup 31/P NMR studies of oriented multilayers formed from isolated sarcoplasmic reticulum and reconstituted sarcoplasmic reticulum: evidence that ''boundary-layer'' phospholipid is not immobilized
- Brookhaven National Lab., Upton, NY
Studies were made of the angular dependence of the /sup 31/P NMR signal from oriented sarcoplasmic reticulum membranes. Similar spectra were obtained from oriented reconstituted sarcoplasmic reticulum membranes with lipid-to-protein ratios ranging from 42.1 to 110.1 and from oriented bilayer membranes formed from sarcoplasmic reticulum phospholipids. The dependence of the /sup 31/P NMR spectra on the alignment of the membranes with respect to the magnetic field was used to draw two conclusions about the motion of the phospholipid molecules that contribute to the observed spectra. First, the phosphate group and the two adjacent methylene groups are able to rotate rapidly (i.e., faster than 10/sup -5/ s) around the normal to the plane of the membrane. Second, calibration experiments showed that all (100 +/- 7%) of the phospholipid molecules in the membrane can be accounted for in the observed spectra. Thus, essentially all the phospholipid molecules in the sarcoplasmic reticulum and the reconstituted sarcoplasmic reticulum membranes have the same motion in the polar headgroup region as found in model bilayer membranes. (JMT)
- OSTI ID:
- 5608219
- Journal Information:
- Biophys. J.; (United States), Journal Name: Biophys. J.; (United States) Vol. 37:1; ISSN BIOJA
- Country of Publication:
- United States
- Language:
- English
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59 BASIC BIOLOGICAL SCIENCES
ESTERS
ISOTOPES
LIGHT NUCLEI
LIPIDS
MAGNETIC RESONANCE
MEMBRANES
MUSCLES
NMR SPECTRA
NUCLEAR MAGNETIC RESONANCE
NUCLEI
ODD-EVEN NUCLEI
ORGANIC COMPOUNDS
ORGANIC PHOSPHORUS COMPOUNDS
PHOSPHOLIPIDS
PHOSPHORUS 31
PHOSPHORUS ISOTOPES
PROTEINS
RESONANCE
SPECTRA
STABLE ISOTOPES
STRUCTURAL CHEMICAL ANALYSIS