Pre-transition effects mediate forces of assembly between transmembrane proteins
We present a mechanism for a generic, powerful force of assembly and mobility for transmembrane proteins in lipid bilayers. This force is a pre-transition (or pre-melting) effect for the first-order transition between ordered and disordered phases in the membrane. Using large-scale molecular simulat...
| Main Authors: | , , , , |
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| Format: | Article |
| Language: | English |
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eLife Sciences Publications Ltd
2016-02-01
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| Series: | eLife |
| Subjects: | |
| Online Access: | https://elifesciences.org/articles/13150 |
| _version_ | 1811235860157300736 |
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| author | Shachi Katira Kranthi K Mandadapu Suriyanarayanan Vaikuntanathan Berend Smit David Chandler |
| author_facet | Shachi Katira Kranthi K Mandadapu Suriyanarayanan Vaikuntanathan Berend Smit David Chandler |
| author_sort | Shachi Katira |
| collection | DOAJ |
| description | We present a mechanism for a generic, powerful force of assembly and mobility for transmembrane proteins in lipid bilayers. This force is a pre-transition (or pre-melting) effect for the first-order transition between ordered and disordered phases in the membrane. Using large-scale molecular simulation, we show that a protein with hydrophobic thickness equal to that of the disordered phase embedded in an ordered bilayer stabilizes a microscopic order–disorder interface. The stiffness of that interface is finite. When two such proteins approach each other, they assemble because assembly reduces the net interfacial energy. Analogous to the hydrophobic effect, we refer to this phenomenon as the 'orderphobic effect'. The effect is mediated by proximity to the order–disorder phase transition and the size and hydrophobic mismatch of the protein. The strength and range of forces arising from this effect are significantly larger than those that could arise from membrane elasticity for the membranes considered. |
| first_indexed | 2024-04-12T11:59:19Z |
| format | Article |
| id | doaj.art-a35c22f2dc4741ceb8aa58b543dc5d2f |
| institution | Directory Open Access Journal |
| issn | 2050-084X |
| language | English |
| last_indexed | 2024-04-12T11:59:19Z |
| publishDate | 2016-02-01 |
| publisher | eLife Sciences Publications Ltd |
| record_format | Article |
| series | eLife |
| spelling | doaj.art-a35c22f2dc4741ceb8aa58b543dc5d2f2022-12-22T03:33:54ZengeLife Sciences Publications LtdeLife2050-084X2016-02-01510.7554/eLife.13150Pre-transition effects mediate forces of assembly between transmembrane proteinsShachi Katira0Kranthi K Mandadapu1Suriyanarayanan Vaikuntanathan2Berend Smit3David Chandler4Department of Chemistry, University of California, Berkeley, Berkeley, United StatesChemical Sciences Division, Lawrence Berkeley National Laboratory, Berkeley, United States; Department of Chemical and Biomolecular Engineering, University of California, Berkeley, Berkeley, United StatesDepartment of Chemistry, University of Chicago, Chicago, United StatesDepartment of Chemistry, University of California, Berkeley, Berkeley, United States; Department of Chemical and Biomolecular Engineering, University of California, Berkeley, Berkeley, United States; Laboratory of Molecular Simulation, Institut des Sciences et Ingénierie Chimiques, Ecole Polytechnique Fédérale de Lausanne, Sion, SwitzerlandDepartment of Chemistry, University of California, Berkeley, Berkeley, United StatesWe present a mechanism for a generic, powerful force of assembly and mobility for transmembrane proteins in lipid bilayers. This force is a pre-transition (or pre-melting) effect for the first-order transition between ordered and disordered phases in the membrane. Using large-scale molecular simulation, we show that a protein with hydrophobic thickness equal to that of the disordered phase embedded in an ordered bilayer stabilizes a microscopic order–disorder interface. The stiffness of that interface is finite. When two such proteins approach each other, they assemble because assembly reduces the net interfacial energy. Analogous to the hydrophobic effect, we refer to this phenomenon as the 'orderphobic effect'. The effect is mediated by proximity to the order–disorder phase transition and the size and hydrophobic mismatch of the protein. The strength and range of forces arising from this effect are significantly larger than those that could arise from membrane elasticity for the membranes considered.https://elifesciences.org/articles/13150lipid bilayersphase transitionhydrophobic mismatchorderphobeorderphobic effect |
| spellingShingle | Shachi Katira Kranthi K Mandadapu Suriyanarayanan Vaikuntanathan Berend Smit David Chandler Pre-transition effects mediate forces of assembly between transmembrane proteins eLife lipid bilayers phase transition hydrophobic mismatch orderphobe orderphobic effect |
| title | Pre-transition effects mediate forces of assembly between transmembrane proteins |
| title_full | Pre-transition effects mediate forces of assembly between transmembrane proteins |
| title_fullStr | Pre-transition effects mediate forces of assembly between transmembrane proteins |
| title_full_unstemmed | Pre-transition effects mediate forces of assembly between transmembrane proteins |
| title_short | Pre-transition effects mediate forces of assembly between transmembrane proteins |
| title_sort | pre transition effects mediate forces of assembly between transmembrane proteins |
| topic | lipid bilayers phase transition hydrophobic mismatch orderphobe orderphobic effect |
| url | https://elifesciences.org/articles/13150 |
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