Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9

Detalhes bibliográficos
Autor(a) principal: Duarte, Daniel Fernandes
Data de Publicação: 2013
Tipo de documento: Dissertação
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: http://hdl.handle.net/10362/10387
Resumo: Dissertação para obtenção do Grau de Mestre em Bioquímica Estrutural e Funcional
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spelling Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9Dissertação para obtenção do Grau de Mestre em Bioquímica Estrutural e FuncionalMost single domain proteins have the ability to fold spontaneously into a precise, functional three-dimensional structure in seconds or less. Understanding how this transition occurs will not only help to uncover the way in which an amino acid sequence encodes the corresponding structure but is also likely to provide insight into the folding/unfolding transitions that many proteins undergo as part of their normal functioning. The characterization of these states is particularly important because they often play crucial roles in folding and misfolding processes, responsible for many human neurodegenerative diseases, such as Alzheimer’s and Parkinson’s diseases. In this work, two well characterized proteins, Colicin immunity proteins Im7 and Im9, where used as model for a structural study involving two different approaches to promote their denaturation/unfolding. Im7 and Im9 share a high sequence and structural homology, but despite that fact they fold with different kinetic mechanism in vitro. By using 1H-15N HSQC spectra as a main tool, we have undertaken a comparative study to identify the residues more affected during the denaturation process of Im7 and Im9 promoted by a physical effect, temperature increase, and by a chemical agent, urea. Our aim was to detect possible similarities that could give insight into the aspects that govern folding/unfolding transitions. The results from the temperature study show that the residues most perturbed with increasing temperature are mostly located in loop regions between helices, while urea targets preferably residues that are accessible and solvent exposed. Our study, points out that the ends of well-structured helices can concertedly unfold without entering the mid region residues in the same unfolding process. There seems to be a correlation between dynamic residues (most affected by temperature) and the residues in the regions most perturbed by urea. The results shown that entire loop regions on both proteins may act as concerted units during the unfolding process, and contribute for favorable interactions that delimit and stabilize native-like structural features on the urea-unfolded state, allowing buried regions to be less solvent exposed.Fundação para a Ciência e a Tecnologia - PEst-C/EQB/LA0006/2011 and Project no. PTDC/QUI-QUI/098892/2008Faculdade de Ciências e TecnologiaCabrita, EuricoFigueiredo, ÂngeloRUNDuarte, Daniel Fernandes2013-09-11T09:11:02Z20132013-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/masterThesisapplication/pdfhttp://hdl.handle.net/10362/10387enginfo: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:RCAAP2024-03-11T03:44:08Zoai:run.unl.pt:10362/10387Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-20T03:19:26.643192Repositório 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 Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9
title Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9
spellingShingle Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9
Duarte, Daniel Fernandes
title_short Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9
title_full Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9
title_fullStr Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9
title_full_unstemmed Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9
title_sort Structural characterization of the urea-unfolded state of Colicin Immunity Protein Im7 and Im9
author Duarte, Daniel Fernandes
author_facet Duarte, Daniel Fernandes
author_role author
dc.contributor.none.fl_str_mv Cabrita, Eurico
Figueiredo, Ângelo
RUN
dc.contributor.author.fl_str_mv Duarte, Daniel Fernandes
description Dissertação para obtenção do Grau de Mestre em Bioquímica Estrutural e Funcional
publishDate 2013
dc.date.none.fl_str_mv 2013-09-11T09:11:02Z
2013
2013-01-01T00:00:00Z
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/10362/10387
url http://hdl.handle.net/10362/10387
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.publisher.none.fl_str_mv Faculdade de Ciências e Tecnologia
publisher.none.fl_str_mv Faculdade de Ciências e Tecnologia
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
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