On the interaction of small molecules with hemoproteins: Sperm whale myoglobin
The spin label TEMPO does not show a binding to myoglobin molecule in solution. This is probably due to the fact that this protein does not have a hydrophobic pocket large enough to accommodate the TEMPO molecule. In the crystal the spin label is bound and two kinds of spectra are observed: one isot...
Published in: | Il Nuovo Cimento D |
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1985
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Online Access: | http://hdl.handle.net/11449/63716 https://doi.org/10.1007/BF02452548 |
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ftunivespir:oai:repositorio.unesp.br:11449/63716 2023-07-02T03:33:47+02:00 On the interaction of small molecules with hemoproteins: Sperm whale myoglobin Baffa, O. Tabak, M. Nascimento, O. R. Ruggiero, J. Universidade Estadual Paulista (UNESP) 1985-06-01 516-526 http://hdl.handle.net/11449/63716 https://doi.org/10.1007/BF02452548 eng eng Il Nuovo Cimento D http://dx.doi.org/10.1007/BF02452548 Il Nuovo Cimento D, v. 5, n. 6, p. 516-526, 1985. 0392-6737 http://hdl.handle.net/11449/63716 doi:10.1007/BF02452548 2-s2.0-51249175097 closedAccess Molecular biophysics info:eu-repo/semantics/article 1985 ftunivespir https://doi.org/10.1007/BF02452548 2023-06-12T16:13:08Z The spin label TEMPO does not show a binding to myoglobin molecule in solution. This is probably due to the fact that this protein does not have a hydrophobic pocket large enough to accommodate the TEMPO molecule. In the crystal the spin label is bound and two kinds of spectra are observed: one isotropic and the other anisotropic. The anisotropic site is probably an intermolecular one. The correlation time for the label in the crystal is very sensitive to temperature showing a transition near 30 °C. This change can be explained as a result of the conformational change observed for myoglobin near this temperature: the motion of the spin label becomes more restricted below this temperature. Change in hydration is the probable cause of this structural change. The changes in the EPR spectra of the anisotropic label suggest that it is bound near the first layers of protein in the crystal. © 1985 Societá Italiana di Fisica. Article in Journal/Newspaper Sperm whale Universidade Estadual Paulista São Paulo: Repositório Institucional UNESP Il Nuovo Cimento D 5 6 516 526 |
institution |
Open Polar |
collection |
Universidade Estadual Paulista São Paulo: Repositório Institucional UNESP |
op_collection_id |
ftunivespir |
language |
English |
topic |
Molecular biophysics |
spellingShingle |
Molecular biophysics Baffa, O. Tabak, M. Nascimento, O. R. Ruggiero, J. On the interaction of small molecules with hemoproteins: Sperm whale myoglobin |
topic_facet |
Molecular biophysics |
description |
The spin label TEMPO does not show a binding to myoglobin molecule in solution. This is probably due to the fact that this protein does not have a hydrophobic pocket large enough to accommodate the TEMPO molecule. In the crystal the spin label is bound and two kinds of spectra are observed: one isotropic and the other anisotropic. The anisotropic site is probably an intermolecular one. The correlation time for the label in the crystal is very sensitive to temperature showing a transition near 30 °C. This change can be explained as a result of the conformational change observed for myoglobin near this temperature: the motion of the spin label becomes more restricted below this temperature. Change in hydration is the probable cause of this structural change. The changes in the EPR spectra of the anisotropic label suggest that it is bound near the first layers of protein in the crystal. © 1985 Societá Italiana di Fisica. |
author2 |
Universidade Estadual Paulista (UNESP) |
format |
Article in Journal/Newspaper |
author |
Baffa, O. Tabak, M. Nascimento, O. R. Ruggiero, J. |
author_facet |
Baffa, O. Tabak, M. Nascimento, O. R. Ruggiero, J. |
author_sort |
Baffa, O. |
title |
On the interaction of small molecules with hemoproteins: Sperm whale myoglobin |
title_short |
On the interaction of small molecules with hemoproteins: Sperm whale myoglobin |
title_full |
On the interaction of small molecules with hemoproteins: Sperm whale myoglobin |
title_fullStr |
On the interaction of small molecules with hemoproteins: Sperm whale myoglobin |
title_full_unstemmed |
On the interaction of small molecules with hemoproteins: Sperm whale myoglobin |
title_sort |
on the interaction of small molecules with hemoproteins: sperm whale myoglobin |
publishDate |
1985 |
url |
http://hdl.handle.net/11449/63716 https://doi.org/10.1007/BF02452548 |
genre |
Sperm whale |
genre_facet |
Sperm whale |
op_relation |
Il Nuovo Cimento D http://dx.doi.org/10.1007/BF02452548 Il Nuovo Cimento D, v. 5, n. 6, p. 516-526, 1985. 0392-6737 http://hdl.handle.net/11449/63716 doi:10.1007/BF02452548 2-s2.0-51249175097 |
op_rights |
closedAccess |
op_doi |
https://doi.org/10.1007/BF02452548 |
container_title |
Il Nuovo Cimento D |
container_volume |
5 |
container_issue |
6 |
container_start_page |
516 |
op_container_end_page |
526 |
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1770273870846099456 |