Conformational dynamics of a lipid−interacting protein: MD simulations of saposin B
Saposin B is a water soluble alpha-helical protein which can bind to membranes and extract selected lipids, especially cerebroside sulfates. The X-ray structure of saposin B is homodimeric. There are two conformations of the dimer in the crystal-one with a closed central cavity (the AB dimer) and on...
| Main Authors: | , , , |
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| Format: | Journal article |
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2007
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| _version_ | 1826278301865345024 |
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| author | Stokeley, D Bemporad, D Gavaghan, D Sansom, M |
| author_facet | Stokeley, D Bemporad, D Gavaghan, D Sansom, M |
| author_sort | Stokeley, D |
| collection | OXFORD |
| description | Saposin B is a water soluble alpha-helical protein which can bind to membranes and extract selected lipids, especially cerebroside sulfates. The X-ray structure of saposin B is homodimeric. There are two conformations of the dimer in the crystal-one with a closed central cavity (the AB dimer) and one (the CD dimer) with a more open cavity. We have conducted a series of short (5 ns) molecular dynamics simulations of saposin B, starting from both the AB and CD conformations and with/wi |
| first_indexed | 2024-03-06T23:41:54Z |
| format | Journal article |
| id | oxford-uuid:6f9be737-8df6-4920-845f-0ae06d488a12 |
| institution | University of Oxford |
| last_indexed | 2024-03-06T23:41:54Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:6f9be737-8df6-4920-845f-0ae06d488a122022-03-26T19:31:39ZConformational dynamics of a lipid−interacting protein: MD simulations of saposin BJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:6f9be737-8df6-4920-845f-0ae06d488a12Department of Computer Science2007Stokeley, DBemporad, DGavaghan, DSansom, MSaposin B is a water soluble alpha-helical protein which can bind to membranes and extract selected lipids, especially cerebroside sulfates. The X-ray structure of saposin B is homodimeric. There are two conformations of the dimer in the crystal-one with a closed central cavity (the AB dimer) and one (the CD dimer) with a more open cavity. We have conducted a series of short (5 ns) molecular dynamics simulations of saposin B, starting from both the AB and CD conformations and with/wi |
| spellingShingle | Stokeley, D Bemporad, D Gavaghan, D Sansom, M Conformational dynamics of a lipid−interacting protein: MD simulations of saposin B |
| title | Conformational dynamics of a lipid−interacting protein: MD simulations of saposin B |
| title_full | Conformational dynamics of a lipid−interacting protein: MD simulations of saposin B |
| title_fullStr | Conformational dynamics of a lipid−interacting protein: MD simulations of saposin B |
| title_full_unstemmed | Conformational dynamics of a lipid−interacting protein: MD simulations of saposin B |
| title_short | Conformational dynamics of a lipid−interacting protein: MD simulations of saposin B |
| title_sort | conformational dynamics of a lipid interacting protein md simulations of saposin b |
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