Role of aromatic interactions in amyloid formation by islet amyloid polypeptide

Biochemistry

Volumn 52, Issue 2, 2013, Pages 333-342

  Tu, Ling Hsien ^a   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBRIL; AMYLOID FORMATION; AROMATIC INTERACTIONS; AROMATIC RESIDUES; DOUBLE MUTANTS; FIBRIL STRUCTURE; NON-ADDITIVE; SINGLE MUTANT; TYPE-2 DIABETES; WILD TYPES;

AMINO ACIDS; AROMATIC COMPOUNDS; AROMATIZATION; HYDROPHOBICITY; POLYPEPTIDES;

GLYCOPROTEINS;

AMINO ACID; AMYLIN; AMYLOID; LEUCINE;

ALPHA HELIX; ARTICLE; BETA SHEET; HYDROPHOBICITY; MUTATION; NON INSULIN DEPENDENT DIABETES MELLITUS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; WILD TYPE;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; DIABETES MELLITUS, TYPE 2; HUMANS; ISLET AMYLOID POLYPEPTIDE; KINETICS; LEUCINE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PHENYLALANINE; PROPANOLS; TYROSINE;

EID: 84872579755     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi3014278     Document Type: Article

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