Quantitative analysis of helix-coil transition of block copolypeptide, Glu12-Ala12, by combined use of CD and NMR spectroscopy

Biopolymers - Peptide Science Section

Volumn 80, Issue 2-3, 2005, Pages 225-232

  Yamazaki, Toshimasa ^a   Furuya, Hidemine ^b   Watanabe, Takeshi ^b   Miyachi, Sayaka ^b   Nishiuchi, Yuji ^c   Nishio, Hideki ^c   Abe, Akihiro ^d  

^a NATIONAL INSTITUTE OF AGROBIOLOGICAL SCIENCES   (Japan)

^b TOKYO INSTITUTE OF TECHNOLOGY   (Japan)

^c Protein Research Foundation   (Japan)

^d TOKYO POLYTECHNIC UNIVERSITY   (Japan)

Author keywords

Block copolypeptide; CD; Helix coil transition; NMR; Thermodynamics

Indexed keywords

BLOCK COPOLYMERS; CONFORMATIONS; DISPERSIONS; ENTHALPY; HYDROGEN BONDS; PH EFFECTS; RESONANCE;

CD SPECTROSCOPY; HELIX-COIL TRANSITIONS; INTRAMOLECULAR HYDROGEN BOND; NUCLEAR OVERHAUSER EFFECT (NOE);

POLYPEPTIDES;

ALANINE; AMIDE; COPOLYMER; POLY(GLUTAMIC ACID CO ALANINE); POLYALANINE; POLYGLUTAMIC ACID; POLYLYSINE; POLYPEPTIDE; PROTON; SODIUM CHLORIDE; UNCLASSIFIED DRUG;

ALPHA HELIX; AMINO TERMINAL SEQUENCE; AQUEOUS SOLUTION; ARTICLE; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; ENTHALPY; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; NUCLEAR OVERHAUSER EFFECT; PH; QUANTITATIVE ANALYSIS; TEMPERATURE; THERMODYNAMICS;

AMINO ACID SEQUENCE; CIRCULAR DICHROISM; HYDROGEN-ION CONCENTRATION; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; THERMODYNAMICS;

EID: 20344404972     PISSN: 00063525     EISSN: None     Source Type: Journal    
DOI: 10.1002/bip.20206     Document Type: Article

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