Deamidation accelerates amyloid formation and alters amylin fiber structure

Journal of the American Chemical Society

Volumn 134, Issue 30, 2012, Pages 12658-12667

  Dunkelberger, Emily B ^a   Buchanan, Lauren E ^a   Marek, Peter ^b   Cao, Ping ^b   Raleigh, Daniel P ^b   Zanni, Martin T ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMYLOID FIBERS; AMYLOID FORMATION; CAUSATIVE AGENTS; CONVENTIONAL METHODS; DEAMIDATED; DEAMIDATION; FIBER STRUCTURES; ISOTOPE LABELING; LARGE PARTS; N-TERMINALS; NON-ENZYMATIC; POST-TRANSLATIONAL MODIFICATIONS; POTENTIAL SITES; SITE-SPECIFIC; STANDARD METHOD; STRUCTURAL MODELS; STRUCTURAL STUDIES; TWO-DIMENSIONAL INFRARED (2D IR); TYPE-2 DIABETES;

AMINO ACIDS; DEGRADATION; FIBERS; GLYCOPROTEINS; ISOTOPES; MODEL STRUCTURES;

PROTEINS;

AMYLIN; AMYLOID;

AMINO TERMINAL SEQUENCE; ARTICLE; BETA SHEET; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; DEAMINATION; ESTERIFICATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; HUMAN; IN VITRO STUDY; INFRARED SPECTROSCOPY; ISOTOPE LABELING; NON INSULIN DEPENDENT DIABETES MELLITUS; PROTEIN AGGREGATION; PROTEIN PROCESSING; TRANSMISSION ELECTRON MICROSCOPY;

AMIDES; AMYLOID; DIABETES MELLITUS, TYPE 2; HUMANS; ISLET AMYLOID POLYPEPTIDE; MODELS, MOLECULAR; PROTEIN PROCESSING, POST-TRANSLATIONAL; PROTEIN STRUCTURE, SECONDARY; SPECTROPHOTOMETRY, INFRARED;

EID: 84864448462     PISSN: 00027863     EISSN: 15205126     Source Type: Journal    
DOI: 10.1021/ja3039486     Document Type: Article

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