Structural polymorphism of human islet amyloid polypeptide (hIAPP) oligomers highlights the importance of interfacial residue interactions

Biomacromolecules

Volumn 12, Issue 1, 2011, Pages 210-220

  Zhao, Jun ^a   Yu, Xiang ^a   Liang, Guizhao ^a,b   Zheng, Jie ^a  

^a The University of Akron   (United States)

^b CHONGQING UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AGGREGATION MECHANISM; AMYLOID PLAQUES; CELL DYSFUNCTION; CROSS-SECTION AREA; DIABETES PATIENTS; EXPERIMENTAL DATA; GLOBULAR STRUCTURE; HUMAN ISLETS; HYDROPHOBIC INTERACTIONS; INTERMOLECULAR INTERACTIONS; INTRINSIC NATURE; MAIN COMPONENT; MOLECULAR DYNAMICS SIMULATIONS; N-TERMINALS; PANCREATIC ISLET; POLAR INTERACTIONS; SIDE-CHAIN INTERACTIONS; SIMULATED MODEL; SOLID STATE NMR; SOLVATION ENERGY; STRUCTURAL POLYMORPHISMS; STRUCTURAL STABILITIES; THREE-LAYER; TOXIC SPECIES; TYPE II;

CELL DEATH; GLYCOPROTEINS; HYDROPHOBICITY; MOLECULAR DYNAMICS; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; OLIGOMERS; OPTIMIZATION; PEPTIDES; POLYMORPHISM; STABILITY;

COMPUTER SIMULATION;

AMYLIN; OLIGOMER;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; ENZYME POLYMORPHISM; EXPERIMENTAL MODEL; HUMAN; HYDROPHOBIC INTERACTION CHROMATOGRAPHY; MOLECULAR DYNAMICS; MOLECULAR WEIGHT; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN PROTEIN INTERACTION; SIMULATION; SOLID STATE; SOLVATION;

AMYLOID; COMPUTER SIMULATION; DIABETES MELLITUS, TYPE 2; HUMANS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; ISLET AMYLOID POLYPEPTIDE; MODELS, MOLECULAR; PANCREAS; PROTEIN MULTIMERIZATION; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY;

EID: 78651268241     PISSN: 15257797     EISSN: 15264602     Source Type: Journal    
DOI: 10.1021/bm101159p     Document Type: Article

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