Conformational preferences of the amylin nucleation site in SDS micelles: An NMR study

Biopolymers

Volumn 69, Issue 1, 2003, Pages 29-41

  Mascioni, Alessandro ^a,b   Porcelli, Fernando ^b   Ilangovan, Udayar ^c   Ramamoorthy, Ayyalusamy ^c   Veglia, Gianluigi ^a,d  

^a University of Minnesota   (United States)

^b UNIVERSITY OF TUSCIA   (Italy)

^c UNIVERSITY OF MICHIGAN   (United States)

^d UNIVERSITY OF MINNESOTA   (United States)

Author keywords

Amylin; Human islet amyloid polypeptide; Micelles; Orientation; Solution NMR

Indexed keywords

AMINO ACIDS; CELL MEMBRANES; CONFORMATIONS; HYDROPHOBICITY; MICELLES; MOLECULAR DYNAMICS; MOLECULAR STRUCTURE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEATION; TOXICITY;

PEPTIDES;

HORMONES;

AMYLIN;

AMINO TERMINAL SEQUENCE; ARTICLE; BILAYER MEMBRANE; CARBOXY TERMINAL SEQUENCE; CYTOTOXICITY; HORMONE BINDING; HORMONE STRUCTURE; HUMAN; HYDROPHOBICITY; MEMBRANE BINDING; MICELLE; NON INSULIN DEPENDENT DIABETES MELLITUS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PANCREAS ISLET BETA CELL; PEPTIDE ANALYSIS;

AMINO ACID SEQUENCE; AMYLOID; ANIMALS; HUMANS; MAGNETIC RESONANCE SPECTROSCOPY; MICELLES; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION; RATS; SEQUENCE ALIGNMENT; SEQUENCE HOMOLOGY, AMINO ACID; SODIUM DODECYL SULFATE;

EID: 0038374923     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10305     Document Type: Article

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