The powerful high pressure tool for protein conformational studies

Detalhes bibliográficos
Autor(a) principal: Marchal,S.
Data de Publicação: 2005
Outros Autores: Torrent,J., Masson,P., Kornblatt,J.M., Tortora,P., Fusi,P., Lange,R., Balny,C.
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Brazilian Journal of Medical and Biological Research
Texto Completo: http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800004
Resumo: The pressure behavior of proteins may be summarized as a the pressure-induced disordering of their structures. This thermodynamic parameter has effects on proteins that are similar but not identical to those induced by temperature, the other thermodynamic parameter. Of particular importance are the intermolecular interactions that follow partial protein unfolding and that give rise to the formation of fibrils. Because some proteins do not form fibrils under pressure, these observations can be related to the shape of the stability diagram. Weak interactions which are differently affected by hydrostatic pressure or temperature play a determinant role in protein stability. Pressure acts on the 2º, 3º and 4º structures of proteins which are maintained by electrostatic and hydrophobic interactions and by hydrogen bonds. We present some typical examples of how pressure affects the tertiary structure of proteins (the case of prion proteins), induces unfolding (ataxin), is a convenient tool to study enzyme dissociation (enolase), and provides arguments to understand the role of the partial volume of an enzyme (butyrylcholinesterase). This approach may have important implications for the understanding of the basic mechanism of protein diseases and for the development of preventive and therapeutic measures.
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spelling The powerful high pressure tool for protein conformational studiesHigh pressurePrion proteinAmyloidAtaxinEnolaseButyrylcholinesteraseThe pressure behavior of proteins may be summarized as a the pressure-induced disordering of their structures. This thermodynamic parameter has effects on proteins that are similar but not identical to those induced by temperature, the other thermodynamic parameter. Of particular importance are the intermolecular interactions that follow partial protein unfolding and that give rise to the formation of fibrils. Because some proteins do not form fibrils under pressure, these observations can be related to the shape of the stability diagram. Weak interactions which are differently affected by hydrostatic pressure or temperature play a determinant role in protein stability. Pressure acts on the 2º, 3º and 4º structures of proteins which are maintained by electrostatic and hydrophobic interactions and by hydrogen bonds. We present some typical examples of how pressure affects the tertiary structure of proteins (the case of prion proteins), induces unfolding (ataxin), is a convenient tool to study enzyme dissociation (enolase), and provides arguments to understand the role of the partial volume of an enzyme (butyrylcholinesterase). This approach may have important implications for the understanding of the basic mechanism of protein diseases and for the development of preventive and therapeutic measures.Associação Brasileira de Divulgação Científica2005-08-01info:eu-repo/semantics/articleinfo:eu-repo/semantics/publishedVersiontext/htmlhttp://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800004Brazilian Journal of Medical and Biological Research v.38 n.8 2005reponame:Brazilian Journal of Medical and Biological Researchinstname:Associação Brasileira de Divulgação Científica (ABDC)instacron:ABDC10.1590/S0100-879X2005000800004info:eu-repo/semantics/openAccessMarchal,S.Torrent,J.Masson,P.Kornblatt,J.M.Tortora,P.Fusi,P.Lange,R.Balny,C.eng2005-07-30T00:00:00Zoai:scielo:S0100-879X2005000800004Revistahttps://www.bjournal.org/https://old.scielo.br/oai/scielo-oai.phpbjournal@terra.com.br||bjournal@terra.com.br1414-431X0100-879Xopendoar:2005-07-30T00:00Brazilian Journal of Medical and Biological Research - Associação Brasileira de Divulgação Científica (ABDC)false
dc.title.none.fl_str_mv The powerful high pressure tool for protein conformational studies
title The powerful high pressure tool for protein conformational studies
spellingShingle The powerful high pressure tool for protein conformational studies
Marchal,S.
High pressure
Prion protein
Amyloid
Ataxin
Enolase
Butyrylcholinesterase
title_short The powerful high pressure tool for protein conformational studies
title_full The powerful high pressure tool for protein conformational studies
title_fullStr The powerful high pressure tool for protein conformational studies
title_full_unstemmed The powerful high pressure tool for protein conformational studies
title_sort The powerful high pressure tool for protein conformational studies
author Marchal,S.
author_facet Marchal,S.
Torrent,J.
Masson,P.
Kornblatt,J.M.
Tortora,P.
Fusi,P.
Lange,R.
Balny,C.
author_role author
author2 Torrent,J.
Masson,P.
Kornblatt,J.M.
Tortora,P.
Fusi,P.
Lange,R.
Balny,C.
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Marchal,S.
Torrent,J.
Masson,P.
Kornblatt,J.M.
Tortora,P.
Fusi,P.
Lange,R.
Balny,C.
dc.subject.por.fl_str_mv High pressure
Prion protein
Amyloid
Ataxin
Enolase
Butyrylcholinesterase
topic High pressure
Prion protein
Amyloid
Ataxin
Enolase
Butyrylcholinesterase
description The pressure behavior of proteins may be summarized as a the pressure-induced disordering of their structures. This thermodynamic parameter has effects on proteins that are similar but not identical to those induced by temperature, the other thermodynamic parameter. Of particular importance are the intermolecular interactions that follow partial protein unfolding and that give rise to the formation of fibrils. Because some proteins do not form fibrils under pressure, these observations can be related to the shape of the stability diagram. Weak interactions which are differently affected by hydrostatic pressure or temperature play a determinant role in protein stability. Pressure acts on the 2º, 3º and 4º structures of proteins which are maintained by electrostatic and hydrophobic interactions and by hydrogen bonds. We present some typical examples of how pressure affects the tertiary structure of proteins (the case of prion proteins), induces unfolding (ataxin), is a convenient tool to study enzyme dissociation (enolase), and provides arguments to understand the role of the partial volume of an enzyme (butyrylcholinesterase). This approach may have important implications for the understanding of the basic mechanism of protein diseases and for the development of preventive and therapeutic measures.
publishDate 2005
dc.date.none.fl_str_mv 2005-08-01
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800004
url http://old.scielo.br/scielo.php?script=sci_arttext&pid=S0100-879X2005000800004
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 10.1590/S0100-879X2005000800004
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv text/html
dc.publisher.none.fl_str_mv Associação Brasileira de Divulgação Científica
publisher.none.fl_str_mv Associação Brasileira de Divulgação Científica
dc.source.none.fl_str_mv Brazilian Journal of Medical and Biological Research v.38 n.8 2005
reponame:Brazilian Journal of Medical and Biological Research
instname:Associação Brasileira de Divulgação Científica (ABDC)
instacron:ABDC
instname_str Associação Brasileira de Divulgação Científica (ABDC)
instacron_str ABDC
institution ABDC
reponame_str Brazilian Journal of Medical and Biological Research
collection Brazilian Journal of Medical and Biological Research
repository.name.fl_str_mv Brazilian Journal of Medical and Biological Research - Associação Brasileira de Divulgação Científica (ABDC)
repository.mail.fl_str_mv bjournal@terra.com.br||bjournal@terra.com.br
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