Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse
Abstract The structural properties and the conformational dynamics of antarctic fish Notothenia coriiceps and mouse metallothioneins were studied by Fourier‐transform infrared and fluorescence spectroscopy. Infrared data revealed that the secondary structure of the two metallothioneins is similar to...
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crwiley:10.1002/prot.10050 2023-12-03T10:12:29+01:00 Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse Capasso, Clemente Abugo, Omoefe Tanfani, Fabio Scire, Andrea Carginale, Vincenzo Scudiero, Rosaria Parisi, Elio D'Auria, Sabato 2002 http://dx.doi.org/10.1002/prot.10050 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.10050 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.10050 en eng Wiley http://onlinelibrary.wiley.com/termsAndConditions#vor Proteins: Structure, Function, and Bioinformatics volume 46, issue 3, page 259-267 ISSN 0887-3585 1097-0134 Molecular Biology Biochemistry Structural Biology journal-article 2002 crwiley https://doi.org/10.1002/prot.10050 2023-11-09T13:48:31Z Abstract The structural properties and the conformational dynamics of antarctic fish Notothenia coriiceps and mouse metallothioneins were studied by Fourier‐transform infrared and fluorescence spectroscopy. Infrared data revealed that the secondary structure of the two metallothioneins is similar to that of other metallothioneins, most of which lack periodical secondary structure elements such as α‐helices and β‐sheets. However, the infrared spectra of the N. coriiceps metallothionein indicated the presence of a band, which for its typical position in the spectrum and for its sensitivity to temperature was assigned to α‐helices whose content resulted in 5% of the total secondary structure of the protein. The short α‐helix found in N. coriiceps metallothionein showed an onset of denaturation at 30°C and a T m at 48°C. The data suggest that in N. coriiceps metallothionein a particular cysteine is involved in the α‐helix and in the metal‐thiolate complex. Moreover, infrared spectra revealed that both proteins investigated possess a structure largely accessible to the solvent. The time‐resolved fluorescence data show that N. coriiceps metallothionein possesses a more flexible structure than mouse metallothionein. The spectroscopic data are discussed in terms of the biological function of the metallothioneins. Proteins 2002;46:259–267. © 2002 Wiley‐Liss, Inc. Article in Journal/Newspaper Antarc* Antarctic Wiley Online Library (via Crossref) Antarctic The Antarctic Proteins: Structure, Function, and Genetics 46 3 259 267 |
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Wiley Online Library (via Crossref) |
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crwiley |
language |
English |
topic |
Molecular Biology Biochemistry Structural Biology |
spellingShingle |
Molecular Biology Biochemistry Structural Biology Capasso, Clemente Abugo, Omoefe Tanfani, Fabio Scire, Andrea Carginale, Vincenzo Scudiero, Rosaria Parisi, Elio D'Auria, Sabato Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse |
topic_facet |
Molecular Biology Biochemistry Structural Biology |
description |
Abstract The structural properties and the conformational dynamics of antarctic fish Notothenia coriiceps and mouse metallothioneins were studied by Fourier‐transform infrared and fluorescence spectroscopy. Infrared data revealed that the secondary structure of the two metallothioneins is similar to that of other metallothioneins, most of which lack periodical secondary structure elements such as α‐helices and β‐sheets. However, the infrared spectra of the N. coriiceps metallothionein indicated the presence of a band, which for its typical position in the spectrum and for its sensitivity to temperature was assigned to α‐helices whose content resulted in 5% of the total secondary structure of the protein. The short α‐helix found in N. coriiceps metallothionein showed an onset of denaturation at 30°C and a T m at 48°C. The data suggest that in N. coriiceps metallothionein a particular cysteine is involved in the α‐helix and in the metal‐thiolate complex. Moreover, infrared spectra revealed that both proteins investigated possess a structure largely accessible to the solvent. The time‐resolved fluorescence data show that N. coriiceps metallothionein possesses a more flexible structure than mouse metallothionein. The spectroscopic data are discussed in terms of the biological function of the metallothioneins. Proteins 2002;46:259–267. © 2002 Wiley‐Liss, Inc. |
format |
Article in Journal/Newspaper |
author |
Capasso, Clemente Abugo, Omoefe Tanfani, Fabio Scire, Andrea Carginale, Vincenzo Scudiero, Rosaria Parisi, Elio D'Auria, Sabato |
author_facet |
Capasso, Clemente Abugo, Omoefe Tanfani, Fabio Scire, Andrea Carginale, Vincenzo Scudiero, Rosaria Parisi, Elio D'Auria, Sabato |
author_sort |
Capasso, Clemente |
title |
Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse |
title_short |
Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse |
title_full |
Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse |
title_fullStr |
Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse |
title_full_unstemmed |
Stability and conformational dynamics of metallothioneins from the antarctic fish Notothenia coriiceps and mouse |
title_sort |
stability and conformational dynamics of metallothioneins from the antarctic fish notothenia coriiceps and mouse |
publisher |
Wiley |
publishDate |
2002 |
url |
http://dx.doi.org/10.1002/prot.10050 https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1002%2Fprot.10050 https://onlinelibrary.wiley.com/doi/pdf/10.1002/prot.10050 |
geographic |
Antarctic The Antarctic |
geographic_facet |
Antarctic The Antarctic |
genre |
Antarc* Antarctic |
genre_facet |
Antarc* Antarctic |
op_source |
Proteins: Structure, Function, and Bioinformatics volume 46, issue 3, page 259-267 ISSN 0887-3585 1097-0134 |
op_rights |
http://onlinelibrary.wiley.com/termsAndConditions#vor |
op_doi |
https://doi.org/10.1002/prot.10050 |
container_title |
Proteins: Structure, Function, and Genetics |
container_volume |
46 |
container_issue |
3 |
container_start_page |
259 |
op_container_end_page |
267 |
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1784259068145172480 |