Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations

Detalhes bibliográficos
Autor(a) principal: Reddy, P. Madhusudhana
Data de Publicação: 2015
Outros Autores: Taha, M., Sharma, Y. V. R. Kameshwar, Venkatesu, Pannuru, Lee, Ming-Jer
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10773/19360
Resumo: Here, circular dichroism (CD) spectroscopy, fluorescence spectroscopy, UV-Vis spectroscopy, SDS-PAGE, substrate SDS-PAGE, and molecular dynamics (MD) simulations techniques have been employed to understand the structural behavioral changes of trypsin (MW: 19.72 kDa, source: digestive system of adult Indian major carp, Catla C. catla) in the presence of various chemical environments. The stability of the trypsin can be increased by stabilizers, including trimethylamine N-oxide (TMAO), proline, and betaine, without affecting its native structure. Trypsin has shown unusual high thermal stability in the presence of betaine. Further, these experimental results were confirmed by means of MD simulations. The present results explicitly elucidated that the behavior of a co-solvent may vary depending upon the type of the protein.
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spelling Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulationsTRIMETHYLAMINE-N-OXIDEUREA-INDUCED DENATURATIONALPHA-CHYMOTRYPSINTRYPTOPHAN FLUORESCENCEGUANIDINE-HYDROCHLORIDEPROTEIN STABILITYGLYCINE BETAINEPREFERENTIAL INTERACTIONSCIRCULAR-DICHROISMOSMOLYTESHere, circular dichroism (CD) spectroscopy, fluorescence spectroscopy, UV-Vis spectroscopy, SDS-PAGE, substrate SDS-PAGE, and molecular dynamics (MD) simulations techniques have been employed to understand the structural behavioral changes of trypsin (MW: 19.72 kDa, source: digestive system of adult Indian major carp, Catla C. catla) in the presence of various chemical environments. The stability of the trypsin can be increased by stabilizers, including trimethylamine N-oxide (TMAO), proline, and betaine, without affecting its native structure. Trypsin has shown unusual high thermal stability in the presence of betaine. Further, these experimental results were confirmed by means of MD simulations. The present results explicitly elucidated that the behavior of a co-solvent may vary depending upon the type of the protein.ROYAL SOC CHEMISTRY2017-12-07T19:10:04Z2015-01-01T00:00:00Z2015info:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10773/19360eng2046-206910.1039/c5ra01302jReddy, P. MadhusudhanaTaha, M.Sharma, Y. V. R. KameshwarVenkatesu, PannuruLee, Ming-Jerinfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2024-02-22T11:37:35Zoai:ria.ua.pt:10773/19360Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T02:54:09.331993Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
title Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
spellingShingle Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
Reddy, P. Madhusudhana
TRIMETHYLAMINE-N-OXIDE
UREA-INDUCED DENATURATION
ALPHA-CHYMOTRYPSIN
TRYPTOPHAN FLUORESCENCE
GUANIDINE-HYDROCHLORIDE
PROTEIN STABILITY
GLYCINE BETAINE
PREFERENTIAL INTERACTIONS
CIRCULAR-DICHROISM
OSMOLYTES
title_short Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
title_full Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
title_fullStr Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
title_full_unstemmed Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
title_sort Quantifying the co-solvent effects on trypsin from the digestive system of carp Catla catla by biophysical techniques and molecular dynamics simulations
author Reddy, P. Madhusudhana
author_facet Reddy, P. Madhusudhana
Taha, M.
Sharma, Y. V. R. Kameshwar
Venkatesu, Pannuru
Lee, Ming-Jer
author_role author
author2 Taha, M.
Sharma, Y. V. R. Kameshwar
Venkatesu, Pannuru
Lee, Ming-Jer
author2_role author
author
author
author
dc.contributor.author.fl_str_mv Reddy, P. Madhusudhana
Taha, M.
Sharma, Y. V. R. Kameshwar
Venkatesu, Pannuru
Lee, Ming-Jer
dc.subject.por.fl_str_mv TRIMETHYLAMINE-N-OXIDE
UREA-INDUCED DENATURATION
ALPHA-CHYMOTRYPSIN
TRYPTOPHAN FLUORESCENCE
GUANIDINE-HYDROCHLORIDE
PROTEIN STABILITY
GLYCINE BETAINE
PREFERENTIAL INTERACTIONS
CIRCULAR-DICHROISM
OSMOLYTES
topic TRIMETHYLAMINE-N-OXIDE
UREA-INDUCED DENATURATION
ALPHA-CHYMOTRYPSIN
TRYPTOPHAN FLUORESCENCE
GUANIDINE-HYDROCHLORIDE
PROTEIN STABILITY
GLYCINE BETAINE
PREFERENTIAL INTERACTIONS
CIRCULAR-DICHROISM
OSMOLYTES
description Here, circular dichroism (CD) spectroscopy, fluorescence spectroscopy, UV-Vis spectroscopy, SDS-PAGE, substrate SDS-PAGE, and molecular dynamics (MD) simulations techniques have been employed to understand the structural behavioral changes of trypsin (MW: 19.72 kDa, source: digestive system of adult Indian major carp, Catla C. catla) in the presence of various chemical environments. The stability of the trypsin can be increased by stabilizers, including trimethylamine N-oxide (TMAO), proline, and betaine, without affecting its native structure. Trypsin has shown unusual high thermal stability in the presence of betaine. Further, these experimental results were confirmed by means of MD simulations. The present results explicitly elucidated that the behavior of a co-solvent may vary depending upon the type of the protein.
publishDate 2015
dc.date.none.fl_str_mv 2015-01-01T00:00:00Z
2015
2017-12-07T19:10:04Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv http://hdl.handle.net/10773/19360
url http://hdl.handle.net/10773/19360
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2046-2069
10.1039/c5ra01302j
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv ROYAL SOC CHEMISTRY
publisher.none.fl_str_mv ROYAL SOC CHEMISTRY
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
institution RCAAP
reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
repository.mail.fl_str_mv
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