Aromatic interactions are not required for amyloid fibril formation by islet amyloid polypeptide but do influence the rate of fibril formation and fibril morphology

Biochemistry

Volumn 46, Issue 11, 2007, Pages 3255-3261

  Marek, Peter ^a   Abedini, Andisheh ^a   Song, BenBen ^a   Kanungo, Mandakini ^b   Johnson, Megan E ^a   Gupta, Ruchi ^a   Zaman, Warda ^a   Wong, Stanislaus S ^a,b   Raleigh, Daniel P ^a  

^a STONY BROOK UNIVERSITY   (United States)

^b BROOKHAVEN NATIONAL LABORATORY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AROMATIC COMPOUNDS; ATOMIC FORCE MICROSCOPY; DISEASES; HYDROPHOBICITY; POLYPEPTIDES; PROTEINS; TRANSMISSION ELECTRON MICROSCOPY;

AMYLOID FIBRILS; AROMATIC INTERACTIONS; FIBRIL FORMATION; PHENYLALANINES;

BIOLOGICAL MEMBRANES;

AMYLIN; AMYLOID; LEUCINE; MUTANT PROTEIN; PHENYLALANINE; POLYPEPTIDE; TYROSINE;

AMINO ACID SUBSTITUTION; ARTICLE; ATOMIC FORCE MICROSCOPY; CIRCULAR DICHROISM; CONTROLLED STUDY; HYDROPHOBICITY; MOLECULAR INTERACTION; NON INSULIN DEPENDENT DIABETES MELLITUS; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ASSEMBLY; PROTEIN PROTEIN INTERACTION; PROTEIN STABILITY; TRANSMISSION ELECTRON MICROSCOPY;

AMINO ACIDS, AROMATIC; AMYLOID; HUMANS; MICROSCOPY, ATOMIC FORCE; MICROSCOPY, ELECTRON, TRANSMISSION;

EID: 33947369859     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0621967     Document Type: Article

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