Fluorescence studies of internal rotation in apohemoglobin α-chains

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

doi:10.1016/0003-9861(84)90018-3

Fluorescence studies of internal rotation in apohemoglobin α-chains

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

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19 Scopus citations

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 language	English (US)
Pages (from-to)	519-524
Number of pages	6
Journal	Archives of Biochemistry and Biophysics
Volume	228
Issue number	2
DOIs	https://doi.org/10.1016/0003-9861(84)90018-3
State	Published - Feb 1 1984
Externally published	Yes

ASJC Scopus subject areas

Biophysics
Biochemistry
Molecular Biology

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10.1016/0003-9861(84)90018-3

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title = "Fluorescence studies of internal rotation in apohemoglobin α-chains",

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.",

author = "Jose Oton and Dionigio Franchi and Steiner, {Robert F.} and Clara Fronticelli and Asuncion Martinez and Enrico Bucci",

note = "Funding Information: This work was supported in part by NIH Grants HL13164 and AM30322. Computer time and facilities were supported in part by the Computer Network of the University of Maryland.",

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T1 - Fluorescence studies of internal rotation in apohemoglobin α-chains

AU - Oton, Jose

AU - Franchi, Dionigio

AU - Steiner, Robert F.

AU - Fronticelli, Clara

AU - Martinez, Asuncion

AU - Bucci, Enrico

N1 - Funding Information: This work was supported in part by NIH Grants HL13164 and AM30322. Computer time and facilities were supported in part by the Computer Network of the University of Maryland.

PY - 1984/2/1

Y1 - 1984/2/1

N2 - 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.

AB - 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.

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Fluorescence studies of internal rotation in apohemoglobin α-chains

Abstract

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