A de novo designed 11 kDa polypeptide: Model for amyloidogenic intrinsically disordered proteins

Biopolymers

Volumn 93, Issue 7, 2010, Pages 607-618

  Topilina, Natalya I ^a   Ermolenkov, Vladimir V ^a   Sikirzhytski, Vitali ^a   Higashiya, Seiichiro ^a   Lednev, Igor K ^a   Welch, John T ^a  

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

Amyloid fibril; Intrinsically disordered protein; Model repetitive polypeptide; Protein folding and aggregation; Raman spectroscopy

Indexed keywords

AMYLOID FIBRIL; CHARGED AMINO ACIDS; CONCENTRATION-DEPENDENT; DEEP UV; DISORDERED PROTEINS; FOLDING KINETICS; FUNCTIONALIZED; INTRINSICALLY DISORDERED PROTEIN; LAG PHASE; NEUTRAL PH; SECONDARY STRUCTURES;

AMINO ACIDS; GLYCOPROTEINS; IONIC STRENGTH; ORGANIC ACIDS; PROTEIN FOLDING; RAMAN SCATTERING; RAMAN SPECTROSCOPY;

POLYPEPTIDES;

ALANINE; AMYLOID PROTEIN; GLUTAMIC ACID; GLYCINE; HISTIDINE; POLYPEPTIDE; TYROSINE;

ARTICLE; BETA SHEET; CONTROLLED STUDY; IONIC STRENGTH; KINETICS; NONHUMAN; PH; PROTEIN AGGREGATION; PROTEIN DEFECT; PROTEIN FOLDING; PROTEIN SECONDARY STRUCTURE; RAMAN SPECTROMETRY; ULTRAVIOLET RADIATION; ULTRAVIOLET SPECTROSCOPY;

AMYLOID; ANIMALS; HUMANS; HYDROGEN-ION CONCENTRATION; KINETICS; MODELS, CHEMICAL; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; SPECTRUM ANALYSIS, RAMAN;

EID: 77953979171     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.21412     Document Type: Article

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