β-Sheet folding of 11-kDa fibrillogenic polypeptide is completely aggregation driven

Biopolymers

Volumn 86, Issue 4, 2007, Pages 261-264

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

^a STATE UNIVERSITY OF NEW YORK   (United States)

Author keywords

Amyloid fibril; Protein folding; Protein secondary structure; Raman spectroscopy

Indexed keywords

AMYLOID FIBRIL; PROTEIN SECONDARY STRUCTURE; SEEDING;

AMINO ACIDS; GENETIC ENGINEERING; PH EFFECTS; PROTEIN FOLDING; PROTONATION; RAMAN SPECTROSCOPY;

POLYPEPTIDES;

GLUTAMIC ACID; HISTIDINE; POLYPEPTIDE;

ARTICLE; ATOMIC FORCE MICROSCOPY; HYDROPHOBICITY; MOLECULAR WEIGHT; PH MEASUREMENT; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STRUCTURE; TRANSMISSION ELECTRON MICROSCOPY;

HYDROGEN-ION CONCENTRATION; KINETICS; MOLECULAR WEIGHT; PEPTIDES; PROTEIN FOLDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN STRUCTURE, SECONDARY; SPECTRUM ANALYSIS, RAMAN;

EID: 34447579289     PISSN: 00063525     EISSN: 10970282     Source Type: Journal    
DOI: 10.1002/bip.20730     Document Type: Article

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