Fluorescence studies of internal rotation in apohemoglobin α-chains

Jose Oton, Dionigio Franchi, Robert F. Steiner, Clara Fronticelli, Asuncion Martinez, Enrico Bucci

Research output: Contribution to journalArticle

Abstract

The molecular dynamics of the apo α-chain of human hemoglobin have been examined using three different fluorescent probes, as well as by circular dichroism. All of these criteria are consistent with a significant loss of organized structure and molecular rigidity for the apo derivative. The apo α-chain thus contrasts with the apo β-chain, which retains considerable rigidity and organized structure.

Original languageEnglish (US)
Pages (from-to)519-524
Number of pages6
JournalArchives of Biochemistry and Biophysics
Volume228
Issue number2
DOIs
StatePublished - Feb 1 1984
Externally publishedYes

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Molecular Dynamics Simulation
Circular Dichroism
Molecular Structure
Fluorescent Dyes
Rigidity
Hemoglobins
Fluorescence
Molecular dynamics
Derivatives
apohemoglobin

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Fluorescence studies of internal rotation in apohemoglobin α-chains. / Oton, Jose; Franchi, Dionigio; Steiner, Robert F.; Fronticelli, Clara; Martinez, Asuncion; Bucci, Enrico.

In: Archives of Biochemistry and Biophysics, Vol. 228, No. 2, 01.02.1984, p. 519-524.

Research output: Contribution to journalArticle

Oton, Jose ; Franchi, Dionigio ; Steiner, Robert F. ; Fronticelli, Clara ; Martinez, Asuncion ; Bucci, Enrico. / Fluorescence studies of internal rotation in apohemoglobin α-chains. In: Archives of Biochemistry and Biophysics. 1984 ; Vol. 228, No. 2. pp. 519-524.
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