Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin: A 1H-NMR and electronic absorbance study

Daniela Delli Castelli, Elena Lovera, Paolo Ascenzi, Mauro Fasano

Research output: Contribution to journalArticle

3 Citations (Scopus)

Abstract

The effect of urea concentration on the backbone solution structure of the cyanide derivative of ferric Caretta caretta myoglobin (at pH 5.4) is reported. By addition of urea, sequential and long-range nuclear Overhauser effects (NOEs) are gradually lost. By using the residual NOE constraints to build the molecular model, a picture of the unfolding pathway was obtained. When the urea concentration is raised to 2.2 M, helices A and B appear largely disordered; helices C, D, and F loose structural constraints at 3.0 M urea. At urea concentration

Original languageEnglish
Pages (from-to)2273-2276
Number of pages4
JournalProtein Science
Volume11
Issue number9
DOIs
Publication statusPublished - Sep 2002

Fingerprint

Turtles
Myoglobin
Urea
Nuclear magnetic resonance
Molecular Models
Cyanides
Proton Magnetic Resonance Spectroscopy
Derivatives

Keywords

  • Caretta caretta
  • Nuclear magnetic resonance
  • Sea turtle myoglobin
  • Unfolding
  • Urea

ASJC Scopus subject areas

  • Biochemistry

Cite this

Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin : A 1H-NMR and electronic absorbance study. / Castelli, Daniela Delli; Lovera, Elena; Ascenzi, Paolo; Fasano, Mauro.

In: Protein Science, Vol. 11, No. 9, 09.2002, p. 2273-2276.

Research output: Contribution to journalArticle

Castelli, Daniela Delli ; Lovera, Elena ; Ascenzi, Paolo ; Fasano, Mauro. / Unfolding of the loggerhead sea turtle (Caretta caretta) myoglobin : A 1H-NMR and electronic absorbance study. In: Protein Science. 2002 ; Vol. 11, No. 9. pp. 2273-2276.
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