Insertion and assembly of membrane proteins via simulation.
Interactions of lipids are central to the folding and stability of membrane proteins. Coarse-grained molecular dynamics simulations have been used to reveal the mechanisms of self-assembly of protein/membrane and protein/detergent complexes for representatives of two classes of membrane protein, nam...
| Principais autores: | , |
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| Formato: | Journal article |
| Idioma: | English |
| Publicado em: |
2006
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| _version_ | 1826303136651804672 |
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| author | Bond, P Sansom, MS |
| author_facet | Bond, P Sansom, MS |
| author_sort | Bond, P |
| collection | OXFORD |
| description | Interactions of lipids are central to the folding and stability of membrane proteins. Coarse-grained molecular dynamics simulations have been used to reveal the mechanisms of self-assembly of protein/membrane and protein/detergent complexes for representatives of two classes of membrane protein, namely, glycophorin (a simple alpha-helical bundle) and OmpA (a beta-barrel). The accuracy of the coarse-grained simulations is established via comparison with the equivalent atomistic simulations of self-assembly of protein/detergent micelles. The simulation of OmpA/bilayer self-assembly reveals how a folded outer membrane protein can be inserted in a bilayer. The glycophorin/bilayer simulation supports the two-state model of membrane folding, in which transmembrane helix insertion precedes dimer self-assembly within a bilayer. The simulations also suggest that a dynamic equilibrium exists between the glycophorin helix monomer and dimer within a bilayer. The simulated glycophorin helix dimer is remarkably close in structure to that revealed by NMR. Thus, coarse-grained methods may help to define mechanisms of membrane protein (re)folding and will prove suitable for simulation of larger scale dynamic rearrangements of biological membranes. |
| first_indexed | 2024-03-07T05:58:04Z |
| format | Journal article |
| id | oxford-uuid:eb368eb1-dc1c-4b4a-b318-19f6bb1007c2 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-07T05:58:04Z |
| publishDate | 2006 |
| record_format | dspace |
| spelling | oxford-uuid:eb368eb1-dc1c-4b4a-b318-19f6bb1007c22022-03-27T11:07:57ZInsertion and assembly of membrane proteins via simulation.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:eb368eb1-dc1c-4b4a-b318-19f6bb1007c2EnglishSymplectic Elements at Oxford2006Bond, PSansom, MSInteractions of lipids are central to the folding and stability of membrane proteins. Coarse-grained molecular dynamics simulations have been used to reveal the mechanisms of self-assembly of protein/membrane and protein/detergent complexes for representatives of two classes of membrane protein, namely, glycophorin (a simple alpha-helical bundle) and OmpA (a beta-barrel). The accuracy of the coarse-grained simulations is established via comparison with the equivalent atomistic simulations of self-assembly of protein/detergent micelles. The simulation of OmpA/bilayer self-assembly reveals how a folded outer membrane protein can be inserted in a bilayer. The glycophorin/bilayer simulation supports the two-state model of membrane folding, in which transmembrane helix insertion precedes dimer self-assembly within a bilayer. The simulations also suggest that a dynamic equilibrium exists between the glycophorin helix monomer and dimer within a bilayer. The simulated glycophorin helix dimer is remarkably close in structure to that revealed by NMR. Thus, coarse-grained methods may help to define mechanisms of membrane protein (re)folding and will prove suitable for simulation of larger scale dynamic rearrangements of biological membranes. |
| spellingShingle | Bond, P Sansom, MS Insertion and assembly of membrane proteins via simulation. |
| title | Insertion and assembly of membrane proteins via simulation. |
| title_full | Insertion and assembly of membrane proteins via simulation. |
| title_fullStr | Insertion and assembly of membrane proteins via simulation. |
| title_full_unstemmed | Insertion and assembly of membrane proteins via simulation. |
| title_short | Insertion and assembly of membrane proteins via simulation. |
| title_sort | insertion and assembly of membrane proteins via simulation |
| work_keys_str_mv | AT bondp insertionandassemblyofmembraneproteinsviasimulation AT sansomms insertionandassemblyofmembraneproteinsviasimulation |