1H NMR studies of prototypical helical designer peptides: A comparative study of the amide chemical shift dependency on temperature and polypeptide sequence

International Journal of Peptide and Protein Research

Volumn 47, Issue 6, 1996, Pages 467-476

  Vinogradov, Alex A ^a   Mari, Frank ^a   Humphreys, Robert E ^b   Wright, George E ^b  

^a FLORIDA ATLANTIC UNIVERSITY   (United States)

^b UNIVERSITY OF MASSACHUSETTS MEDICAL SCHOOL   (United States)

Author keywords

'H nuclear magnetic resonance; Amphiphilic; Folding; Helicity; Hydrophobicity

Indexed keywords

PEPTIDE; TRIFLUOROETHANOL;

ARTICLE; CHEMISTRY; HYDROGEN BOND; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEIN CONFORMATION; PROTEIN SECONDARY STRUCTURE; AMINO ACID SEQUENCE; ANTIGEN PRESENTATION; HYDROPHOBICITY; NUCLEAR OVERHAUSER EFFECT; PROTEIN ANALYSIS; PROTON NUCLEAR MAGNETIC RESONANCE;

HYDROGEN BONDING; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDES; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; TRIFLUOROETHANOL;

EID: 0029657923     PISSN: 03678377     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1399-3011.1996.tb01097.x     Document Type: Article

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