Chain-Length Dependence of α-Helix to β-Sheet Transition in Polylysine: Model of Protein Aggregation Studied by Temperature-Tuned FTIR Spectroscopy

Biopolymers

Volumn 73, Issue 4, 2004, Pages 463-469

  Dzwolak, Wojciech ^a   Muraki, Takeshi ^b   Kato, Minoru ^b   Taniguchi, Yoshihiro ^b  

^a INSTITUTE OF HIGH PRESSURE PHYSICS   (Poland)

^b RITSUMEIKAN UNIVERSITY   (Japan)

Author keywords

Amyloid; Fourier transform IR spectroscopy; Poly(L lysine); Protein aggregation

Indexed keywords

CONFORMATIONS; FOURIER TRANSFORM INFRARED SPECTROSCOPY; POLYPEPTIDES; PROTEINS; THERMAL EFFECTS;

METASTABLE PROTEINS; PREASSEMBLIES;

BIOPOLYMERS;

AMYLOID; POLYLYSINE;

ALPHA HELIX; ARTICLE; BETA SHEET; CONFORMATIONAL TRANSITION; INFRARED SPECTROSCOPY; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN INTERACTION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS; TEMPERATURE DEPENDENCE;

MOLECULAR WEIGHT; POLYLYSINE; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE;

EID: 1542724787     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.10582     Document Type: Article

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