Triton X-100 as the 'short-chain lipid' improves the magnetic alignment and stability of membrane proteins in phosphatidylcholine bilayers for oriented-sample solid-state NMR spectroscopy

Journal of the American Chemical Society

Volumn 132, Issue 36, 2010, Pages 12552-12553

  Park, Sang Ho ^a   Opella, Stanley J ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

1-FORMS; BI-LAYER; COAT PROTEINS; EXPERIMENTAL PARAMETERS; MAGNETIC ALIGNMENT; MEMBRANE PROTEINS; MOLAR RATIO; PHOSPHATIDYLCHOLINE BILAYERS; PHOSPHOLIPID BILAYER; SOLID STATE NMR; SOLID-STATE NMR SPECTROSCOPY; SOLUTION NMR; TRITON X-100; WELL-ALIGNED;

BIOLOGICAL MEMBRANES; LIPID BILAYERS; PHOSPHOLIPIDS; PROTEINS; SOLID STATE PHYSICS;

NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY;

COAT PROTEIN; MEMBRANE PROTEIN; PHOSPHATIDYLCHOLINE; SHORT CHAIN FATTY ACID; TRITON X 100;

ARTICLE; BILAYER MEMBRANE; MAGNETISM; MICELLE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PHOSPHOLIPID BILAYER; PROTEIN STABILITY; SOLID STATE;

LIPID BILAYERS; MAGNETIC RESONANCE SPECTROSCOPY; MAGNETICS; MEMBRANE PROTEINS; OCTOXYNOL; PHOSPHATIDYLCHOLINES;

EID: 77956448654     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja1055565     Document Type: Article

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