dorsal/arxiv
View SchemaMembrane-protein interactions in mechanosensitive channels
| Authors | Paul Wiggins, Rob Phillips |
|---|---|
| Categories | |
| ArXiv ID | q-bio/0406021 |
| URL | https://arxiv.org/abs/q-bio/0406021 |
| DOI | 10.1529/biophysj.104.047431 |
Abstract
In this paper, we examine the mechanical role of the lipid bilayer in ion channel conformation and function with specific reference to the case of the mechanosensitive channel of large conductance (MscL). In a recent paper (Wiggins and Phillips, 2004), we argued that mechanotransduction very naturally arises from lipid-protein interactions by invoking a simple analytic model of the MscL channel and the surrounding lipid bilayer. In this paper, we focus on improving and expanding this analytic framework for studying lipid-protein interactions with special attention to MscL. Our goal is to generate simple scaling relations which can be used to provide qualitative understanding of the role of membrane mechanics in protein function and to quantitatively interpret experimental results. For the MscL channel, we find that the free energies induced by lipid-protein interaction are of the same order as the free energy differences between conductance states measured by Sukharev et al. (1999). We therefore conclude that the mechanics of the bilayer plays an essential role in determining the conformation and function of the channel. Finally, we compare the predictions of our model to experimental results from the recent investigations of the MscL channel by Perozo et al. (2002), Powl et al. (2003), Yoshimura et al. (2004), and others and suggest a suite of new experiments.
{
"annotation_id": "df6ee353-29c5-4f9b-a32a-bbaffd174142",
"date_created": "2026-03-02T18:01:31.681000Z",
"date_modified": "2026-03-02T18:01:31.681000Z",
"file_hash": "7adaeeb6d66c97c85121188399c24f05f51302cb104eb123acc1182b360cf88f",
"private": false,
"record": {
"abstract": "In this paper, we examine the mechanical role of the lipid bilayer in ion\nchannel conformation and function with specific reference to the case of the\nmechanosensitive channel of large conductance (MscL). In a recent paper\n(Wiggins and Phillips, 2004), we argued that mechanotransduction very naturally\narises from lipid-protein interactions by invoking a simple analytic model of\nthe MscL channel and the surrounding lipid bilayer. In this paper, we focus on\nimproving and expanding this analytic framework for studying lipid-protein\ninteractions with special attention to MscL. Our goal is to generate simple\nscaling relations which can be used to provide qualitative understanding of the\nrole of membrane mechanics in protein function and to quantitatively interpret\nexperimental results. For the MscL channel, we find that the free energies\ninduced by lipid-protein interaction are of the same order as the free energy\ndifferences between conductance states measured by Sukharev et al. (1999). We\ntherefore conclude that the mechanics of the bilayer plays an essential role in\ndetermining the conformation and function of the channel. Finally, we compare\nthe predictions of our model to experimental results from the recent\ninvestigations of the MscL channel by Perozo et al. (2002), Powl et al. (2003),\nYoshimura et al. (2004), and others and suggest a suite of new experiments.",
"arxiv_id": "q-bio/0406021",
"authors": [
"Paul Wiggins",
"Rob Phillips"
],
"categories": [
"q-bio.BM"
],
"doi": "10.1529/biophysj.104.047431",
"title": "Membrane-protein interactions in mechanosensitive channels",
"url": "https://arxiv.org/abs/q-bio/0406021"
},
"schema_id": "dorsal/arxiv",
"source": {
"execution_id": "20f40e5c-fa49-4967-93f7-a498fe4efec5",
"id": "arXiv Dataset IDs",
"type": "Model",
"variant": "snapshot-2026-03-01",
"version": "0.1.0"
},
"user_id": 1000002
}