Two-dimensional IR spectroscopy and isotope labeling defines the pathway of amyloid formation with residue-specific resolution

Proceedings of the National Academy of Sciences of the United States of America

Volumn 106, Issue 16, 2009, Pages 6614-6619

  Shim, Sang Hee ^a   Gupta, Ruchi ^b   Ling, Yun L ^a   Strasfeld, David B ^a   Raleigh, Daniel P ^b   Zanni, Martin T ^a  

^a UNIVERSITY OF WISCONSIN MADISON   (United States)

^b STONY BROOK UNIVERSITY   (United States)

Author keywords

Aggregation; Amylin; Fibers; Human islet amyloid polypeptide; Nucleation

Indexed keywords

AMYLIN; AMYLOID; AMINO ACID;

AMINO TERMINAL SEQUENCE; ARTICLE; EXPERIMENTAL STUDY; FIBER; HUMAN; IMAGE QUALITY; INFRARED SPECTROSCOPY; ISOTOPE LABELING; KINETICS; METHODOLOGY; MONITORING; NON INSULIN DEPENDENT DIABETES MELLITUS; OPTICAL RESOLUTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN STRUCTURE; TWO DIMENSIONAL IMAGING; AMINO ACID SEQUENCE; CHEMISTRY; INFRARED SPECTROPHOTOMETRY; METABOLISM; MOLECULAR GENETICS; PROTEIN QUATERNARY STRUCTURE; REPRODUCIBILITY;

AMINO ACID SEQUENCE; AMINO ACIDS; AMYLOID; HUMANS; ISOTOPE LABELING; KINETICS; MOLECULAR SEQUENCE DATA; PROTEIN STRUCTURE, QUATERNARY; REPRODUCIBILITY OF RESULTS; SPECTROPHOTOMETRY, INFRARED;

EID: 66149084447     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.0805957106     Document Type: Article

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