Structural features of aquaporin 4 supporting the formation of arrays and junctions in biomembranes. Höfinger, S., Yamamoto, E., Hirano, Y., Zerbetto, F., Narumi, T., Yasuoka, K., & Yasui, M. Biochim. Biophys. Acta, 1818(9):2234-43, 9, 2012. Paper abstract bibtex A limited class of aquaporins has been described to form regular arrays and junctions in membranes. The biological significance of these structures, however, remains uncertain. Here we analyze the underlying physical principles with the help of a computational procedure that takes into account protein-protein as well as protein-membrane interactions. Experimentally observed array/junction structures are systematically (dis)assembled and major driving forces identified. Aquaporin 4 was found to be markedly different from the non-junction forming aquaporin 1. The environmental stabilization resulting from embedding into the biomembrane was identified as the main driving force. This highlights the role of protein-membrane interactions in aquaporin 4. Analysis of the type presented here can help to decipher the biological role of membrane arrays and junctions formed by aquaporin.
@article{
id = {c833f827-d0f9-33bf-86c2-b8903285f617},
title = {Structural features of aquaporin 4 supporting the formation of arrays and junctions in biomembranes.},
type = {article},
year = {2012},
identifiers = {[object Object]},
keywords = {Animals,Aquaporin 4,Aquaporin 4: chemistry,Biophysics,Biophysics: methods,Cattle,Cell Membrane,Cell Membrane: metabolism,Lipids,Lipids: chemistry,Models, Molecular,Molecular Conformation,Molecular Dynamics Simulation,Protein Binding,Protein Interaction Mapping,Protein Interaction Mapping: methods,Protein Structure, Tertiary,Proteins,Proteins: chemistry,Rats,Thermodynamics,Water,Water: chemistry},
created = {2014-12-10T04:09:01.000Z},
pages = {2234-43},
volume = {1818},
websites = {http://www.sciencedirect.com/science/article/pii/S0005273612001319},
month = {9},
accessed = {2014-06-23},
file_attached = {true},
profile_id = {6708b05a-e661-38c6-9bb8-cf4f304b6385},
group_id = {424eb3e1-9b50-35ed-91d3-65c78c3164d7},
last_modified = {2014-12-10T09:11:31.000Z},
read = {false},
starred = {false},
authored = {false},
confirmed = {true},
hidden = {false},
citation_key = {Hofinger2012a},
abstract = {A limited class of aquaporins has been described to form regular arrays and junctions in membranes. The biological significance of these structures, however, remains uncertain. Here we analyze the underlying physical principles with the help of a computational procedure that takes into account protein-protein as well as protein-membrane interactions. Experimentally observed array/junction structures are systematically (dis)assembled and major driving forces identified. Aquaporin 4 was found to be markedly different from the non-junction forming aquaporin 1. The environmental stabilization resulting from embedding into the biomembrane was identified as the main driving force. This highlights the role of protein-membrane interactions in aquaporin 4. Analysis of the type presented here can help to decipher the biological role of membrane arrays and junctions formed by aquaporin.},
bibtype = {article},
author = {Höfinger, Siegfried and Yamamoto, Eiji and Hirano, Yoshinori and Zerbetto, Francesco and Narumi, Tetsu and Yasuoka, Kenji and Yasui, Masato},
journal = {Biochim. Biophys. Acta},
number = {9}
}
Downloads: 0
{"_id":"3XvnAe5Ms4wjccZoD","bibbaseid":"hfinger-yamamoto-hirano-zerbetto-narumi-yasuoka-yasui-structuralfeaturesofaquaporin4supportingtheformationofarraysandjunctionsinbiomembranes-2012","downloads":0,"creationDate":"2014-12-15T00:59:26.380Z","title":"Structural features of aquaporin 4 supporting the formation of arrays and junctions in biomembranes.","author_short":["Höfinger, S.","Yamamoto, E.","Hirano, Y.","Zerbetto, F.","Narumi, T.","Yasuoka, K.","Yasui, M."],"year":2012,"bibtype":"article","biburl":null,"bibdata":{"id":"c833f827-d0f9-33bf-86c2-b8903285f617","title":"Structural features of aquaporin 4 supporting the formation of arrays and junctions in biomembranes.","type":"article","year":"2012","identifiers":"[object Object]","keywords":"Animals,Aquaporin 4,Aquaporin 4: chemistry,Biophysics,Biophysics: methods,Cattle,Cell Membrane,Cell Membrane: metabolism,Lipids,Lipids: chemistry,Models, Molecular,Molecular Conformation,Molecular Dynamics Simulation,Protein Binding,Protein Interaction Mapping,Protein Interaction Mapping: methods,Protein Structure, Tertiary,Proteins,Proteins: chemistry,Rats,Thermodynamics,Water,Water: chemistry","created":"2014-12-10T04:09:01.000Z","pages":"2234-43","volume":"1818","websites":"http://www.sciencedirect.com/science/article/pii/S0005273612001319","month":"9","accessed":"2014-06-23","file_attached":"true","profile_id":"6708b05a-e661-38c6-9bb8-cf4f304b6385","group_id":"424eb3e1-9b50-35ed-91d3-65c78c3164d7","last_modified":"2014-12-10T09:11:31.000Z","read":false,"starred":false,"authored":false,"confirmed":"true","hidden":false,"citation_key":"Hofinger2012a","abstract":"A limited class of aquaporins has been described to form regular arrays and junctions in membranes. The biological significance of these structures, however, remains uncertain. Here we analyze the underlying physical principles with the help of a computational procedure that takes into account protein-protein as well as protein-membrane interactions. Experimentally observed array/junction structures are systematically (dis)assembled and major driving forces identified. Aquaporin 4 was found to be markedly different from the non-junction forming aquaporin 1. The environmental stabilization resulting from embedding into the biomembrane was identified as the main driving force. This highlights the role of protein-membrane interactions in aquaporin 4. Analysis of the type presented here can help to decipher the biological role of membrane arrays and junctions formed by aquaporin.","bibtype":"article","author":"Höfinger, Siegfried and Yamamoto, Eiji and Hirano, Yoshinori and Zerbetto, Francesco and Narumi, Tetsu and Yasuoka, Kenji and Yasui, Masato","journal":"Biochim. Biophys. Acta","number":"9","bibtex":"@article{\n id = {c833f827-d0f9-33bf-86c2-b8903285f617},\n title = {Structural features of aquaporin 4 supporting the formation of arrays and junctions in biomembranes.},\n type = {article},\n year = {2012},\n identifiers = {[object Object]},\n keywords = {Animals,Aquaporin 4,Aquaporin 4: chemistry,Biophysics,Biophysics: methods,Cattle,Cell Membrane,Cell Membrane: metabolism,Lipids,Lipids: chemistry,Models, Molecular,Molecular Conformation,Molecular Dynamics Simulation,Protein Binding,Protein Interaction Mapping,Protein Interaction Mapping: methods,Protein Structure, Tertiary,Proteins,Proteins: chemistry,Rats,Thermodynamics,Water,Water: chemistry},\n created = {2014-12-10T04:09:01.000Z},\n pages = {2234-43},\n volume = {1818},\n websites = {http://www.sciencedirect.com/science/article/pii/S0005273612001319},\n month = {9},\n accessed = {2014-06-23},\n file_attached = {true},\n profile_id = {6708b05a-e661-38c6-9bb8-cf4f304b6385},\n group_id = {424eb3e1-9b50-35ed-91d3-65c78c3164d7},\n last_modified = {2014-12-10T09:11:31.000Z},\n read = {false},\n starred = {false},\n authored = {false},\n confirmed = {true},\n hidden = {false},\n citation_key = {Hofinger2012a},\n abstract = {A limited class of aquaporins has been described to form regular arrays and junctions in membranes. The biological significance of these structures, however, remains uncertain. Here we analyze the underlying physical principles with the help of a computational procedure that takes into account protein-protein as well as protein-membrane interactions. Experimentally observed array/junction structures are systematically (dis)assembled and major driving forces identified. Aquaporin 4 was found to be markedly different from the non-junction forming aquaporin 1. The environmental stabilization resulting from embedding into the biomembrane was identified as the main driving force. This highlights the role of protein-membrane interactions in aquaporin 4. Analysis of the type presented here can help to decipher the biological role of membrane arrays and junctions formed by aquaporin.},\n bibtype = {article},\n author = {Höfinger, Siegfried and Yamamoto, Eiji and Hirano, Yoshinori and Zerbetto, Francesco and Narumi, Tetsu and Yasuoka, Kenji and Yasui, Masato},\n journal = {Biochim. Biophys. Acta},\n number = {9}\n}","author_short":["Höfinger, S.","Yamamoto, E.","Hirano, Y.","Zerbetto, F.","Narumi, T.","Yasuoka, K.","Yasui, M."],"urls":{"Paper":"http://bibbase.org/service/mendeley/a7e4c3bf-9985-3f7f-bdc6-7f9a22a4e887/file/1161e460-2ad0-bfd1-1133-adf1e8d222f6/2012-Structural_features_of_aquaporin_4_supporting_the_formation_of_arrays_and_junctions_in_biomembranes..pdf.pdf"},"bibbaseid":"hfinger-yamamoto-hirano-zerbetto-narumi-yasuoka-yasui-structuralfeaturesofaquaporin4supportingtheformationofarraysandjunctionsinbiomembranes-2012","role":"author","keyword":["Animals","Aquaporin 4","Aquaporin 4: chemistry","Biophysics","Biophysics: methods","Cattle","Cell Membrane","Cell Membrane: metabolism","Lipids","Lipids: chemistry","Models","Molecular","Molecular Conformation","Molecular Dynamics Simulation","Protein Binding","Protein Interaction Mapping","Protein Interaction Mapping: methods","Protein Structure","Tertiary","Proteins","Proteins: chemistry","Rats","Thermodynamics","Water","Water: chemistry"],"downloads":0},"search_terms":["structural","features","aquaporin","supporting","formation","arrays","junctions","biomembranes","höfinger","yamamoto","hirano","zerbetto","narumi","yasuoka","yasui"],"keywords":["animals","aquaporin 4","aquaporin 4: chemistry","biophysics","biophysics: methods","cattle","cell membrane","cell membrane: metabolism","lipids","lipids: chemistry","models","molecular","molecular conformation","molecular dynamics simulation","protein binding","protein interaction mapping","protein interaction mapping: methods","protein structure","tertiary","proteins","proteins: chemistry","rats","thermodynamics","water","water: chemistry"],"authorIDs":[]}