Initial simulation coordinates.
<p><b>A)</b> p7 amino acids and their corresponding position within the protein. <b>B)</b> Two p7 monomers separated (<i>Sep</i> model) and <b>C)</b> extracted from the hexameric structure PDBID 2M6X (initial <i>Bound</i> model config...
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| _version_ | 1849927626857119744 |
|---|---|
| author | Oluwatoyin Campbell (14392137) |
| author2 | Dina Dahhan (22683620) Viviana Monje (2056069) |
| author2_role | author author |
| author_facet | Oluwatoyin Campbell (14392137) Dina Dahhan (22683620) Viviana Monje (2056069) |
| author_role | author |
| dc.creator.none.fl_str_mv | Oluwatoyin Campbell (14392137) Dina Dahhan (22683620) Viviana Monje (2056069) |
| dc.date.none.fl_str_mv | 2025-11-25T18:38:53Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pcbi.1013736.g001 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Initial_simulation_coordinates_/30714701 |
| dc.rights.none.fl_str_mv | CC BY 4.0 info:eu-repo/semantics/openAccess |
| dc.subject.none.fl_str_mv | Biophysics Biochemistry Cell Biology Genetics Molecular Biology Biotechnology Cancer Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified Information Systems not elsewhere classified process may help complex transmembrane topology comparing dimer interactions aqueous solution versus promote p7 oligomerization protein residue alignment p7 dimers driven alignment underlie health study demonstrates particularly involving often composed molecular mechanisms key residues hydrophobic contacts hydrogen bonding first helix explain assembly dynamic contributors channel assembly |
| dc.title.none.fl_str_mv | Initial simulation coordinates. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <p><b>A)</b> p7 amino acids and their corresponding position within the protein. <b>B)</b> Two p7 monomers separated (<i>Sep</i> model) and <b>C)</b> extracted from the hexameric structure PDBID 2M6X (initial <i>Bound</i> model configuration). <b>D)</b> Two monomers initially attached by N-termini to the surface of a complex membrane (<i>Surface</i> model) containing DOPC (in green), DPPE (in blue), POPI (in purple), Cholesterol (in black) and DOPS (in orange) (55:21:11:9:4 mol%). Monomers are in the initial positioning seen in replica 1. Water atoms shown with sky blue. Proteins are shown with cartoon representation and differentiated in pink and ice-blue (p1 and p2, respectively); when shown, non-polar residues in white, polar in green and cationic in blue. In snapshots, water and ions are omitted for clarity.</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_072ebf3452a72af9297f8eef09b33444 |
| identifier_str_mv | 10.1371/journal.pcbi.1013736.g001 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30714701 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Initial simulation coordinates.Oluwatoyin Campbell (14392137)Dina Dahhan (22683620)Viviana Monje (2056069)BiophysicsBiochemistryCell BiologyGeneticsMolecular BiologyBiotechnologyCancerBiological Sciences not elsewhere classifiedChemical Sciences not elsewhere classifiedPhysical Sciences not elsewhere classifiedInformation Systems not elsewhere classifiedprocess may helpcomplex transmembrane topologycomparing dimer interactionsaqueous solution versuspromote p7 oligomerizationprotein residue alignmentp7 dimersdriven alignmentunderlie healthstudy demonstratesparticularly involvingoften composedmolecular mechanismskey residueshydrophobic contactshydrogen bondingfirst helixexplain assemblydynamic contributorschannel assembly<p><b>A)</b> p7 amino acids and their corresponding position within the protein. <b>B)</b> Two p7 monomers separated (<i>Sep</i> model) and <b>C)</b> extracted from the hexameric structure PDBID 2M6X (initial <i>Bound</i> model configuration). <b>D)</b> Two monomers initially attached by N-termini to the surface of a complex membrane (<i>Surface</i> model) containing DOPC (in green), DPPE (in blue), POPI (in purple), Cholesterol (in black) and DOPS (in orange) (55:21:11:9:4 mol%). Monomers are in the initial positioning seen in replica 1. Water atoms shown with sky blue. Proteins are shown with cartoon representation and differentiated in pink and ice-blue (p1 and p2, respectively); when shown, non-polar residues in white, polar in green and cationic in blue. In snapshots, water and ions are omitted for clarity.</p>2025-11-25T18:38:53ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pcbi.1013736.g001https://figshare.com/articles/figure/Initial_simulation_coordinates_/30714701CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307147012025-11-25T18:38:53Z |
| spellingShingle | Initial simulation coordinates. Oluwatoyin Campbell (14392137) Biophysics Biochemistry Cell Biology Genetics Molecular Biology Biotechnology Cancer Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified Information Systems not elsewhere classified process may help complex transmembrane topology comparing dimer interactions aqueous solution versus promote p7 oligomerization protein residue alignment p7 dimers driven alignment underlie health study demonstrates particularly involving often composed molecular mechanisms key residues hydrophobic contacts hydrogen bonding first helix explain assembly dynamic contributors channel assembly |
| status_str | publishedVersion |
| title | Initial simulation coordinates. |
| title_full | Initial simulation coordinates. |
| title_fullStr | Initial simulation coordinates. |
| title_full_unstemmed | Initial simulation coordinates. |
| title_short | Initial simulation coordinates. |
| title_sort | Initial simulation coordinates. |
| topic | Biophysics Biochemistry Cell Biology Genetics Molecular Biology Biotechnology Cancer Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified Information Systems not elsewhere classified process may help complex transmembrane topology comparing dimer interactions aqueous solution versus promote p7 oligomerization protein residue alignment p7 dimers driven alignment underlie health study demonstrates particularly involving often composed molecular mechanisms key residues hydrophobic contacts hydrogen bonding first helix explain assembly dynamic contributors channel assembly |