Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K
Autor(a) principal: | |
---|---|
Data de Publicação: | 2014 |
Tipo de documento: | Dissertação |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10198/11602 |
Resumo: | The main objective of this work is to contribute to the understanding of the molecular interactions between ions and protein groups in aqueous solutions, using amino acids as model compounds, by determining the partial molar volumes of glycine, L-alanine, DL-2-aminobutyric acid and L-valine in aqueous magnesium sulphate solutions. The densities of aqueous solutions of magnesium sulphate (0.1, 0.3, 0.7 and 1.0) mol·kg-1 containing the selected amino acids were measured at (278.15, 288.15, 298.15 and 308.15) K, using a digital density meter. After, the partial molar volumes at infinite di-lution of the amino acids were calculated, and then used to obtain the corresponding transfer volumes and hydration numbers. The dehydration effect on the studied amino acids was observed, increasing temperature or salt molality. The positive values of ∆trVmA suggest that the interactions ion/hydrophilic group (zwitterionic centers) are predominant, and applying the method-ology proposed by Friedman and Krishnan (1973), it was concluded that they are main-ly pairwise. Regarding the alkyl chain effect, the increase of the hydrophobic part of amino acids (glycine > L-alanine > DL-2-aminobutyric > L-valine) does not result in a decreasing trend of the partial molar volumes of transfer. To further analyse the alkyl chain effect of the amino acids, a group contribution meth-od was successfully applied to model the partial molar volumes data. The contribution of the zwitterionic (NH3+, COO-) groups to the value of the standard partial molar vol-ume predominates and increases with increasing magnesium sulphate concentration; in general, the contribution of the alkyl groups is much smaller, having a very weak de-creasing trend with increasing salt molality. |
id |
RCAP_8ade63606194b0e75ee70860699f8663 |
---|---|
oai_identifier_str |
oai:bibliotecadigital.ipb.pt:10198/11602 |
network_acronym_str |
RCAP |
network_name_str |
Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
repository_id_str |
7160 |
spelling |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 KPartial molar volumesAmino acidsHydration numbersElectrolyteThe main objective of this work is to contribute to the understanding of the molecular interactions between ions and protein groups in aqueous solutions, using amino acids as model compounds, by determining the partial molar volumes of glycine, L-alanine, DL-2-aminobutyric acid and L-valine in aqueous magnesium sulphate solutions. The densities of aqueous solutions of magnesium sulphate (0.1, 0.3, 0.7 and 1.0) mol·kg-1 containing the selected amino acids were measured at (278.15, 288.15, 298.15 and 308.15) K, using a digital density meter. After, the partial molar volumes at infinite di-lution of the amino acids were calculated, and then used to obtain the corresponding transfer volumes and hydration numbers. The dehydration effect on the studied amino acids was observed, increasing temperature or salt molality. The positive values of ∆trVmA suggest that the interactions ion/hydrophilic group (zwitterionic centers) are predominant, and applying the method-ology proposed by Friedman and Krishnan (1973), it was concluded that they are main-ly pairwise. Regarding the alkyl chain effect, the increase of the hydrophobic part of amino acids (glycine > L-alanine > DL-2-aminobutyric > L-valine) does not result in a decreasing trend of the partial molar volumes of transfer. To further analyse the alkyl chain effect of the amino acids, a group contribution meth-od was successfully applied to model the partial molar volumes data. The contribution of the zwitterionic (NH3+, COO-) groups to the value of the standard partial molar vol-ume predominates and increases with increasing magnesium sulphate concentration; in general, the contribution of the alkyl groups is much smaller, having a very weak de-creasing trend with increasing salt molality.O principal objetivo deste trabalho é contribuir para a compreensão das interações moleculares entre iões e grupos de proteínas em água, utilizando aminoácidos como compostos modelo, através da determinação dos volumes molares parciais da glicina, L-alanina, DL-2-ácido aminobutírico e L-valina, em soluções aquosas de sulfato de mag-nésio. As densidades das soluções aquosas de sulfato de magnésio (0,1, 0,3, 0,7 e 1,0) mol·kg-1 contendo os aminoácidos selecionados foram medidas a (278,15; 288,15; 298,15 e 308,15) K, usando um densímetro digital. Depois, os volumes molares parciais a diluição infinita dos aminoácidos foram calculados, e, em seguida, utilizados para a obtenção dos correspondentes volumes de transferência e números de hidratação. Observou-se um efeito de desidratação nos aminoácidos estudados, aumentando a tem-peratura ou a molalidade de sal. Os valores positivos de ∆trVmA sugerem que as interações ião/grupo hidrofílico (centros zeuteriónicos) são predominantes, e aplicando a metodologia proposta por Friedman e Krishnan (1973), concluiu-se que ocorrem principalmente entre pares. Relativamente ao efeito da cadeia alquílica, o aumento da parte hidrofóbica dos aminoácidos (glicina > L-alanina > DL-2-ácido aminobutírico > L-valina) não resulta numa diminuição dos volumes molares parciais de transferência. Para analisar melhor o efeito da cadeia alquílica dos aminoácidos, aplicou-se um méto-do de contribuição de grupos para modelar os dados dos volumes molares parciais. A contribuição dos grupos zeuteriónicos (NH3+, COO-) para o valor do volume molar par-cial padrão predomina e aumenta com o aumento da concentração de sulfato de magnésio; em geral, a contribuição dos grupos alquilo é muito menor, tendo uma tendência muito fraca de diminuição com o aumento da molalidade de sal.Ferreira, OlgaPinho, SimãoBiblioteca Digital do IPBMota, Ana Carolina Costa2015-01-20T09:45:26Z201420142014-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10198/11602TID:201456214enginfo: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:RCAAP2023-11-21T10:27:24Zoai:bibliotecadigital.ipb.pt:10198/11602Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T23:02:09.106152Repositório 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 |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K |
title |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K |
spellingShingle |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K Mota, Ana Carolina Costa Partial molar volumes Amino acids Hydration numbers Electrolyte |
title_short |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K |
title_full |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K |
title_fullStr |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K |
title_full_unstemmed |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K |
title_sort |
Partial molar volumes of amino acids in aqueous MgSO4 solutions between 278.15 and 308.15 K |
author |
Mota, Ana Carolina Costa |
author_facet |
Mota, Ana Carolina Costa |
author_role |
author |
dc.contributor.none.fl_str_mv |
Ferreira, Olga Pinho, Simão Biblioteca Digital do IPB |
dc.contributor.author.fl_str_mv |
Mota, Ana Carolina Costa |
dc.subject.por.fl_str_mv |
Partial molar volumes Amino acids Hydration numbers Electrolyte |
topic |
Partial molar volumes Amino acids Hydration numbers Electrolyte |
description |
The main objective of this work is to contribute to the understanding of the molecular interactions between ions and protein groups in aqueous solutions, using amino acids as model compounds, by determining the partial molar volumes of glycine, L-alanine, DL-2-aminobutyric acid and L-valine in aqueous magnesium sulphate solutions. The densities of aqueous solutions of magnesium sulphate (0.1, 0.3, 0.7 and 1.0) mol·kg-1 containing the selected amino acids were measured at (278.15, 288.15, 298.15 and 308.15) K, using a digital density meter. After, the partial molar volumes at infinite di-lution of the amino acids were calculated, and then used to obtain the corresponding transfer volumes and hydration numbers. The dehydration effect on the studied amino acids was observed, increasing temperature or salt molality. The positive values of ∆trVmA suggest that the interactions ion/hydrophilic group (zwitterionic centers) are predominant, and applying the method-ology proposed by Friedman and Krishnan (1973), it was concluded that they are main-ly pairwise. Regarding the alkyl chain effect, the increase of the hydrophobic part of amino acids (glycine > L-alanine > DL-2-aminobutyric > L-valine) does not result in a decreasing trend of the partial molar volumes of transfer. To further analyse the alkyl chain effect of the amino acids, a group contribution meth-od was successfully applied to model the partial molar volumes data. The contribution of the zwitterionic (NH3+, COO-) groups to the value of the standard partial molar vol-ume predominates and increases with increasing magnesium sulphate concentration; in general, the contribution of the alkyl groups is much smaller, having a very weak de-creasing trend with increasing salt molality. |
publishDate |
2014 |
dc.date.none.fl_str_mv |
2014 2014 2014-01-01T00:00:00Z 2015-01-20T09:45:26Z |
dc.type.status.fl_str_mv |
info:eu-repo/semantics/publishedVersion |
dc.type.driver.fl_str_mv |
info:eu-repo/semantics/masterThesis |
format |
masterThesis |
status_str |
publishedVersion |
dc.identifier.uri.fl_str_mv |
http://hdl.handle.net/10198/11602 TID:201456214 |
url |
http://hdl.handle.net/10198/11602 |
identifier_str_mv |
TID:201456214 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
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.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 |
|
_version_ |
1799135259430748160 |