Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin
Membrane proteins are laterally coupled to the surrounding cell membrane through complex interactions that can modulate their function. Here, we directly observe and quantify the dynamics of functioning bacteriorhodopsin (bR) in its native membrane, a crystalline aggregate of bR trimers. We show tha...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2009
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| _version_ | 1797075917934166016 |
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| author | Voitchovsky, K Contera, SA Ryan, J |
| author_facet | Voitchovsky, K Contera, SA Ryan, J |
| author_sort | Voitchovsky, K |
| collection | OXFORD |
| description | Membrane proteins are laterally coupled to the surrounding cell membrane through complex interactions that can modulate their function. Here, we directly observe and quantify the dynamics of functioning bacteriorhodopsin (bR) in its native membrane, a crystalline aggregate of bR trimers. We show that much of a monomer's isomerization energy is mechanically redistributed into the membrane, producing cooperative activity within the trimer while simultaneously generating functionally relevant long-range lateral pressure waves. Our results provide evidence of coordinated short and long-range effects in the cell membrane. © 2009 The Royal Society of Chemistry. |
| first_indexed | 2024-03-06T23:56:58Z |
| format | Journal article |
| id | oxford-uuid:748fcb89-5e3d-446e-9330-a102a437f165 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T23:56:58Z |
| publishDate | 2009 |
| record_format | dspace |
| spelling | oxford-uuid:748fcb89-5e3d-446e-9330-a102a437f1652022-03-26T20:03:44ZLateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsinJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:748fcb89-5e3d-446e-9330-a102a437f165EnglishSymplectic Elements at Oxford2009Voitchovsky, KContera, SARyan, JMembrane proteins are laterally coupled to the surrounding cell membrane through complex interactions that can modulate their function. Here, we directly observe and quantify the dynamics of functioning bacteriorhodopsin (bR) in its native membrane, a crystalline aggregate of bR trimers. We show that much of a monomer's isomerization energy is mechanically redistributed into the membrane, producing cooperative activity within the trimer while simultaneously generating functionally relevant long-range lateral pressure waves. Our results provide evidence of coordinated short and long-range effects in the cell membrane. © 2009 The Royal Society of Chemistry. |
| spellingShingle | Voitchovsky, K Contera, SA Ryan, J Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin |
| title | Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin |
| title_full | Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin |
| title_fullStr | Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin |
| title_full_unstemmed | Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin |
| title_short | Lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin |
| title_sort | lateral coupling and cooperative dynamics in the function of the native membrane protein bacteriorhodopsin |
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