Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems.
<p>The average position of phosphorus atoms is indicated with the red line at 0. Error bars represent standard error across replicas.</p> <p>(TIFF)</p>
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2025
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| _version_ | 1849927626905354240 |
|---|---|
| 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 | 2025-11-25T18:38:35Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pcbi.1013736.s008 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/figure/Distance_of_each_amino_acid_from_the_average_position_of_phosphorus_atoms_in_the_contacting_membrane_leaflet_in_the_i_Surface_i_systems_/30714662 |
| 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 | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems. |
| dc.type.none.fl_str_mv | Image Figure info:eu-repo/semantics/publishedVersion image |
| description | <p>The average position of phosphorus atoms is indicated with the red line at 0. Error bars represent standard error across replicas.</p> <p>(TIFF)</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_38d886cdfb191ae43039a6fcfc6b9260 |
| identifier_str_mv | 10.1371/journal.pcbi.1013736.s008 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30714662 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems.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>The average position of phosphorus atoms is indicated with the red line at 0. Error bars represent standard error across replicas.</p> <p>(TIFF)</p>2025-11-25T18:38:35ZImageFigureinfo:eu-repo/semantics/publishedVersionimage10.1371/journal.pcbi.1013736.s008https://figshare.com/articles/figure/Distance_of_each_amino_acid_from_the_average_position_of_phosphorus_atoms_in_the_contacting_membrane_leaflet_in_the_i_Surface_i_systems_/30714662CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307146622025-11-25T18:38:35Z |
| spellingShingle | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems. 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 | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems. |
| title_full | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems. |
| title_fullStr | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems. |
| title_full_unstemmed | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems. |
| title_short | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems. |
| title_sort | Distance of each amino acid from the average position of phosphorus atoms in the contacting membrane leaflet in the <i>Surface</i> systems. |
| 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 |