Role of amino acid hydrophobicity, aromaticity, and molecular volume on IAPP(20-29) amyloid self-assembly

Proteins: Structure, Function and Bioinformatics

Volumn 80, Issue 4, 2012, Pages 1053-1065

  Doran, Todd M ^a   Kamens, Alissa J ^a   Byrnes, Nadia K ^a   Nilsson, Bradley L ^a  

^a UNIVERSITY OF ROCHESTER   (United States)

Author keywords

Amylin; Amyloid; Aromatic interactions; Islet amyloid polypeptide; Self assembly

Indexed keywords

ALPHA NAPHTHYLALANINE; AMINO ACID; AMYLIN; AMYLOID; AMYLOID BETA PROTEIN; CYCLOHEXYLALANINE; LEUCINE; PENTAFLUOROPHENYLALANINE; PHENYLALANINE; TYROSINE; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMYLOIDOGENICITY; AMYLOIDOSIS; AROMATICITY; ARTICLE; BETA SHEET; CHEMICAL BOND; CONTROLLED STUDY; GENE MUTATION; GEOMETRY; HYDROPHOBICITY; MOLECULAR MECHANICS; PANCREAS ISLET CELL; PRIORITY JOURNAL; PROTEIN ASSEMBLY; PROTEIN FOLDING; THERMODYNAMICS;

1-NAPHTHYLAMINE; AMINO ACID SEQUENCE; AMINO ACIDS, AROMATIC; AMYLOID; CHEMISTRY TECHNIQUES, SYNTHETIC; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; ISLET AMYLOID POLYPEPTIDE; KINETICS; LEUCINE; MODELS, MOLECULAR; MUTATION; PEPTIDE FRAGMENTS; PROTEIN INTERACTION MAPPING; PROTEIN MULTIMERIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; THERMODYNAMICS;

EID: 84857793669     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.24007     Document Type: Article

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