Publicação

Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations

Ver documento

Detalhes bibliográficos
Resumo:"Photosystem II subunit S (PsbS) plays a central role in non-photochemical quenching (NPQ), a key photoprotective mechanism that allows plants to dissipate excess absorbed energy under fluctuating light. Acting as a pH sensor, PsbS undergoes protonation-dependent conformational changes triggered by lumen acidification, but the molecular determinants of its activation and dimerization remain still not fully understood. In this study, we employ constant pH molecular dynamics (CpHMD) simulations to investigate the protonation behaviour, conformational dynamics, and pH-dependent dimerization free energies of PsbS. Protonation states of titratable residues were sampled across a range of pH values (3-8), allowing to construct titration curves and estimate residue pa shifts. These revealed positively shifted pa values for several lumen-exposed glutamates, which can act as pH sensors in the physiological window of pH 5–6. Protonation correlation analysis further indicated the presence of complex networks encompassing both lumenal and stromal residues, suggesting long-range communication across the membrane in both monomeric and dimeric states.(...)"
Autores principais:Vitória, Sara Moreno Jorge
Assunto:PsbS NPQ dimerization pH-sensitive behaviour constant pH molecular dynamics
Ano:2025
País:Portugal
Tipo de documento:dissertação de mestrado
Tipo de acesso:acesso aberto
Instituição associada:Universidade Nova de Lisboa
Idioma:inglês
Origem:Repositório Institucional da UNL
_version_ 1868984257137868800
author Vitória, Sara Moreno Jorge
author_facet Vitória, Sara Moreno Jorge
author_role author
contributor_name_str_mv Baptista, António
RUN
country_str PT
creators_json_txt [{\"Person.name\":\"Vitória, Sara Moreno Jorge\"}]
datacite.contributors.contributor.contributorName.fl_str_mv Baptista, António
RUN
datacite.creators.creator.creatorName.fl_str_mv Vitória, Sara Moreno Jorge
datacite.date.Accepted.fl_str_mv 2025-12-09T00:00:00Z
datacite.date.available.fl_str_mv 2026-04-13T16:41:20Z
datacite.date.embargoed.fl_str_mv 2026-04-13T16:41:20Z
datacite.rights.fl_str_mv http://purl.org/coar/access_right/c_abf2
datacite.subjects.subject.fl_str_mv PsbS
NPQ
dimerization
pH-sensitive behaviour
constant pH molecular dynamics
datacite.titles.title.fl_str_mv Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
dc.contributor.none.fl_str_mv Baptista, António
RUN
dc.creator.none.fl_str_mv Vitória, Sara Moreno Jorge
dc.date.Accepted.fl_str_mv 2025-12-09T00:00:00Z
dc.date.available.fl_str_mv 2026-04-13T16:41:20Z
dc.date.embargoed.fl_str_mv 2026-04-13T16:41:20Z
dc.format.none.fl_str_mv application/pdf
dc.identifier.none.fl_str_mv http://hdl.handle.net/10362/202201
dc.language.none.fl_str_mv eng
dc.rights.cclincense.fl_str_mv http://creativecommons.org/licenses/by/4.0/
dc.rights.none.fl_str_mv http://purl.org/coar/access_right/c_abf2
dc.subject.none.fl_str_mv PsbS
NPQ
dimerization
pH-sensitive behaviour
constant pH molecular dynamics
dc.title.fl_str_mv Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
dc.type.none.fl_str_mv http://purl.org/coar/resource_type/c_bdcc
description "Photosystem II subunit S (PsbS) plays a central role in non-photochemical quenching (NPQ), a key photoprotective mechanism that allows plants to dissipate excess absorbed energy under fluctuating light. Acting as a pH sensor, PsbS undergoes protonation-dependent conformational changes triggered by lumen acidification, but the molecular determinants of its activation and dimerization remain still not fully understood. In this study, we employ constant pH molecular dynamics (CpHMD) simulations to investigate the protonation behaviour, conformational dynamics, and pH-dependent dimerization free energies of PsbS. Protonation states of titratable residues were sampled across a range of pH values (3-8), allowing to construct titration curves and estimate residue pa shifts. These revealed positively shifted pa values for several lumen-exposed glutamates, which can act as pH sensors in the physiological window of pH 5–6. Protonation correlation analysis further indicated the presence of complex networks encompassing both lumenal and stromal residues, suggesting long-range communication across the membrane in both monomeric and dimeric states.(...)"
dirty 0
eu_rights_str_mv openAccess
format masterThesis
fulltext.url.fl_str_mv https://run.unl.pt/bitstreams/4156f6e6-1890-4884-bf11-0118251ffd46/download
id run_348dd3f4ddbced016ceb2e5b9be57ca5
identifier.url.fl_str_mv http://hdl.handle.net/10362/202201
inst_facet_str urn:organizationAcronym:unl{{{_:::_}}}Universidade Nova de Lisboa
instacron_str unl
institution Universidade Nova de Lisboa
instname_str Universidade Nova de Lisboa
language eng
network_acronym_str run
network_name_str Repositório Institucional da UNL
oai_identifier_str oai:run.unl.pt:10362/202201
organization_str_mv urn:organizationAcronym:unl
person_str_mv Vitória, Sara Moreno Jorge
publishDate 2025
repo_facet_str urn:repositoryAcronym:run{{{_:::_}}}Repositório Institucional da UNL
reponame_str Repositório Institucional da UNL
repository_id_str urn:repositoryAcronym:run
service_str_mv urn:repositoryAcronym:run
spelling engeng"Photosystem II subunit S (PsbS) plays a central role in non-photochemical quenching (NPQ), a key photoprotective mechanism that allows plants to dissipate excess absorbed energy under fluctuating light. Acting as a pH sensor, PsbS undergoes protonation-dependent conformational changes triggered by lumen acidification, but the molecular determinants of its activation and dimerization remain still not fully understood. In this study, we employ constant pH molecular dynamics (CpHMD) simulations to investigate the protonation behaviour, conformational dynamics, and pH-dependent dimerization free energies of PsbS. Protonation states of titratable residues were sampled across a range of pH values (3-8), allowing to construct titration curves and estimate residue pa shifts. These revealed positively shifted pa values for several lumen-exposed glutamates, which can act as pH sensors in the physiological window of pH 5–6. Protonation correlation analysis further indicated the presence of complex networks encompassing both lumenal and stromal residues, suggesting long-range communication across the membrane in both monomeric and dimeric states.(...)"application/pdfengStudy of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulationsVitória, Sara Moreno JorgeBaptista, AntónioHostingInstitutionOrganizationalRUNe-mailmailto:run@unl.ptrun@unl.ptURNurn:tid:2041560682026-04-13T16:41:20Z2025-12-092025-09-272025-12-09T00:00:00ZHandlehttp://hdl.handle.net/10362/202201http://purl.org/coar/access_right/c_abf2open accessPsbSNPQdimerizationpH-sensitive behaviourconstant pH molecular dynamics40452875 bytesliteraturehttp://purl.org/coar/resource_type/c_bdccmaster thesis2025-12-09http://creativecommons.org/licenses/by/4.0/http://purl.org/coar/access_right/c_abf2application/pdffulltexthttps://run.unl.pt/bitstreams/4156f6e6-1890-4884-bf11-0118251ffd46/download
spellingShingle Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
Vitória, Sara Moreno Jorge
PsbS
NPQ
dimerization
pH-sensitive behaviour
constant pH molecular dynamics
status SINGLETON
subject.fl_str_mv PsbS
NPQ
dimerization
pH-sensitive behaviour
constant pH molecular dynamics
title Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
title_full Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
title_fullStr Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
title_full_unstemmed Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
title_short Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
title_sort Study of the monomer-dimer equilibrium of the pH-sensing protein PsbS using molecular dynamics simulations
topic PsbS
NPQ
dimerization
pH-sensitive behaviour
constant pH molecular dynamics
topic_facet PsbS
NPQ
dimerization
pH-sensitive behaviour
constant pH molecular dynamics
url http://hdl.handle.net/10362/202201
visible 1