Conformational study of a collagen peptide by 1H NMR spectroscopy: observation of the 14N-1H spin-spin coupling of the Arg guanidinium moiety in the triple-helix structure

FEBS Letters

Volumn 436, Issue 2, 1998, Pages 243-246

  Consonni, Roberto ^a   Santomo, Laura ^a   Tenni, Ruggero ^b   Longhi, Renato ^c   Zetta, Lucia ^a  

^a Lab NMR   (Italy)

^b UNIVERSITY OF PAVIA   (Italy)

^c CNR   (Italy)

Author keywords

14N quadrupolar effect; Collagen; Collagen peptide; Nuclear magnetic resonance; Triple helix stability

Indexed keywords

COLLAGEN; CYANOGEN BROMIDE; GUANIDINE; NITROGEN; PEPTIDE; PROTON;

ARTICLE; ENERGY; HYDROGEN BOND; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTON NUCLEAR MAGNETIC RESONANCE; SPIN LABELING; TRIPLE HELIX;

AMINO ACID SEQUENCE; ANIMALS; ARGININE; CATTLE; COLLAGEN; CYANOGEN BROMIDE; GUANIDINE; HUMANS; HYDROGEN; MOLECULAR SEQUENCE DATA; NITROGEN; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDE FRAGMENTS; PROTEIN CONFORMATION;

EID: 0032475954     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0014-5793(98)01125-9     Document Type: Article

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