List of protein residues and selected atoms to define the tilt angle vectors.
<p>Nomenclature corresponds to the C36m FF [<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1013736#pcbi.1013736.ref037" target="_blank">37</a>,<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1013736#...
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2025
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| _version_ | 1849927626944151552 |
|---|---|
| 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 | 2025-11-25T18:38:25Z |
| dc.identifier.none.fl_str_mv | 10.1371/journal.pcbi.1013736.s003 |
| dc.relation.none.fl_str_mv | https://figshare.com/articles/dataset/List_of_protein_residues_and_selected_atoms_to_define_the_tilt_angle_vectors_/30714644 |
| 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 | List of protein residues and selected atoms to define the tilt angle vectors. |
| dc.type.none.fl_str_mv | Dataset info:eu-repo/semantics/publishedVersion dataset |
| description | <p>Nomenclature corresponds to the C36m FF [<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1013736#pcbi.1013736.ref037" target="_blank">37</a>,<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1013736#pcbi.1013736.ref040" target="_blank">40</a>].</p> <p>(XLSX)</p> |
| eu_rights_str_mv | openAccess |
| id | Manara_9cba5c59ded854e1e3f66e6d937ad673 |
| identifier_str_mv | 10.1371/journal.pcbi.1013736.s003 |
| network_acronym_str | Manara |
| network_name_str | ManaraRepo |
| oai_identifier_str | oai:figshare.com:article/30714644 |
| publishDate | 2025 |
| repository.mail.fl_str_mv | |
| repository.name.fl_str_mv | |
| repository_id_str | |
| rights_invalid_str_mv | CC BY 4.0 |
| spelling | List of protein residues and selected atoms to define the tilt angle vectors.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>Nomenclature corresponds to the C36m FF [<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1013736#pcbi.1013736.ref037" target="_blank">37</a>,<a href="http://www.ploscompbiol.org/article/info:doi/10.1371/journal.pcbi.1013736#pcbi.1013736.ref040" target="_blank">40</a>].</p> <p>(XLSX)</p>2025-11-25T18:38:25ZDatasetinfo:eu-repo/semantics/publishedVersiondataset10.1371/journal.pcbi.1013736.s003https://figshare.com/articles/dataset/List_of_protein_residues_and_selected_atoms_to_define_the_tilt_angle_vectors_/30714644CC BY 4.0info:eu-repo/semantics/openAccessoai:figshare.com:article/307146442025-11-25T18:38:25Z |
| spellingShingle | List of protein residues and selected atoms to define the tilt angle vectors. 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 | List of protein residues and selected atoms to define the tilt angle vectors. |
| title_full | List of protein residues and selected atoms to define the tilt angle vectors. |
| title_fullStr | List of protein residues and selected atoms to define the tilt angle vectors. |
| title_full_unstemmed | List of protein residues and selected atoms to define the tilt angle vectors. |
| title_short | List of protein residues and selected atoms to define the tilt angle vectors. |
| title_sort | List of protein residues and selected atoms to define the tilt angle vectors. |
| 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 |