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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Tác giả chính: Oluwatoyin Campbell (14392137) (author)
Tác giả khác: Dina Dahhan (22683620) (author), Viviana Monje (2056069) (author)
Được phát hành: 2025
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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