Solution structure of amyloid β-peptide(1-40) in a water-micelle environment. Is the membrane-spanning domain where we think it is?

Biochemistry

Volumn 37, Issue 31, 1998, Pages 11064-11077

  Coles, Murray ^a   Bicknell, Wendy ^b   Watson, Rew A ^a   Fairlie, David P ^a   Craik, David J ^a  

^a UNIVERSITY OF QUEENSLAND   (Australia)

^b MONASH UNIVERSITY   (Australia)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID BETA PROTEIN; AMYLOID PRECURSOR PROTEIN; WATER;

ALPHA HELIX; ALZHEIMER DISEASE; ARTICLE; CELL MEMBRANE; MICELLE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN DOMAIN; PROTEIN FOLDING; PROTEIN STRUCTURE;

AMINO ACID SEQUENCE; AMYLOID BETA-PROTEIN; CRYSTALLOGRAPHY, X-RAY; HUMANS; HYDROGEN-ION CONCENTRATION; MEMBRANE PROTEINS; MICELLES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN STRUCTURE, SECONDARY; SODIUM DODECYL SULFATE; SOLUTIONS; WATER;

EID: 0032483035     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi972979f     Document Type: Article

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