The nanodisc: a novel tool for membrane protein studies
A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the...
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| Autor*in: |
Borch, Jonas [verfasserIn] Hamann, Thomas [verfasserIn] |
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E-Artikel |
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| Erschienen: |
Walter de Gruyter ; 2009 |
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| Anmerkung: |
©2009 by Walter de Gruyter Berlin New York |
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10 |
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Walter de Gruyter Online Zeitschriften |
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Enthalten in: Biological chemistry - Berlin [u.a.] : de Gruyter, 1996, 390(2009), 8 vom: 20. Mai, Seite 805-814 |
| Übergeordnetes Werk: |
volume:390 ; year:2009 ; number:8 ; day:20 ; month:05 ; pages:805-814 ; extent:10 |
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| DOI / URN: |
10.1515/BC.2009.091 |
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NLEJ246526734 |
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10.1515/BC.2009.091 doi artikel_Grundlieferung.pp (DE-627)NLEJ246526734 DE-627 ger DE-627 rakwb Borch, Jonas verfasserin aut The nanodisc: a novel tool for membrane protein studies Walter de Gruyter 2009 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2009 by Walter de Gruyter Berlin New York A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein. Walter de Gruyter Online Zeitschriften apolipoprotein A-I cytochrome P450 enzymes membrane proteins nanobiosciences nanolipoprotein particles protein interactions Hamann, Thomas verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 390(2009), 8 vom: 20. Mai, Seite 805-814 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:390 year:2009 number:8 day:20 month:05 pages:805-814 extent:10 https://doi.org/10.1515/BC.2009.091 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 390 2009 8 20 05 805-814 10 |
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10.1515/BC.2009.091 doi artikel_Grundlieferung.pp (DE-627)NLEJ246526734 DE-627 ger DE-627 rakwb Borch, Jonas verfasserin aut The nanodisc: a novel tool for membrane protein studies Walter de Gruyter 2009 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2009 by Walter de Gruyter Berlin New York A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein. Walter de Gruyter Online Zeitschriften apolipoprotein A-I cytochrome P450 enzymes membrane proteins nanobiosciences nanolipoprotein particles protein interactions Hamann, Thomas verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 390(2009), 8 vom: 20. Mai, Seite 805-814 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:390 year:2009 number:8 day:20 month:05 pages:805-814 extent:10 https://doi.org/10.1515/BC.2009.091 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 390 2009 8 20 05 805-814 10 |
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10.1515/BC.2009.091 doi artikel_Grundlieferung.pp (DE-627)NLEJ246526734 DE-627 ger DE-627 rakwb Borch, Jonas verfasserin aut The nanodisc: a novel tool for membrane protein studies Walter de Gruyter 2009 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2009 by Walter de Gruyter Berlin New York A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein. Walter de Gruyter Online Zeitschriften apolipoprotein A-I cytochrome P450 enzymes membrane proteins nanobiosciences nanolipoprotein particles protein interactions Hamann, Thomas verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 390(2009), 8 vom: 20. Mai, Seite 805-814 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:390 year:2009 number:8 day:20 month:05 pages:805-814 extent:10 https://doi.org/10.1515/BC.2009.091 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 390 2009 8 20 05 805-814 10 |
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10.1515/BC.2009.091 doi artikel_Grundlieferung.pp (DE-627)NLEJ246526734 DE-627 ger DE-627 rakwb Borch, Jonas verfasserin aut The nanodisc: a novel tool for membrane protein studies Walter de Gruyter 2009 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2009 by Walter de Gruyter Berlin New York A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein. Walter de Gruyter Online Zeitschriften apolipoprotein A-I cytochrome P450 enzymes membrane proteins nanobiosciences nanolipoprotein particles protein interactions Hamann, Thomas verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 390(2009), 8 vom: 20. Mai, Seite 805-814 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:390 year:2009 number:8 day:20 month:05 pages:805-814 extent:10 https://doi.org/10.1515/BC.2009.091 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 390 2009 8 20 05 805-814 10 |
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10.1515/BC.2009.091 doi artikel_Grundlieferung.pp (DE-627)NLEJ246526734 DE-627 ger DE-627 rakwb Borch, Jonas verfasserin aut The nanodisc: a novel tool for membrane protein studies Walter de Gruyter 2009 10 Text txt rdacontent Computermedien c rdamedia Online-Ressource cr rdacarrier ©2009 by Walter de Gruyter Berlin New York A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein. Walter de Gruyter Online Zeitschriften apolipoprotein A-I cytochrome P450 enzymes membrane proteins nanobiosciences nanolipoprotein particles protein interactions Hamann, Thomas verfasserin aut Enthalten in Biological chemistry Berlin [u.a.] : de Gruyter, 1996 390(2009), 8 vom: 20. Mai, Seite 805-814 (DE-627)NLEJ248235095 (DE-600)1466062-3 1437-4315 nnns volume:390 year:2009 number:8 day:20 month:05 pages:805-814 extent:10 https://doi.org/10.1515/BC.2009.091 Deutschlandweit zugänglich GBV_USEFLAG_U ZDB-1-DGR GBV_NL_ARTICLE AR 390 2009 8 20 05 805-814 10 |
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A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein. ©2009 by Walter de Gruyter Berlin New York |
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A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein. ©2009 by Walter de Gruyter Berlin New York |
| abstract_unstemmed |
A major challenge in the research on membrane-anchored and integral membrane protein complexes is to obtain these in a functionally active, water-soluble, and monodisperse form. This requires the incorporation of the membrane proteins into a native-like membrane or detergent micelle that mimics the properties of the original biological membrane. However, solubilization in detergents or reconstitution in liposomes or supported monolayers sometimes suffers from loss of activity and problematic analyses due to heterogeneity and aggregation. A developing technology termed nanodiscs exploits discoidal phospholipid bilayers encircled by a stabilizing amphipatic helical membrane scaffold protein to reconstitute membranes with integral proteins. After reconstitution, the membrane nanodisc is soluble, stable, and monodisperse. In the present review, we outline the biological inspiration for nanodiscs as discoidal high-density lipoproteins, the assembly and handling of nanodiscs, and finally their diverse biochemical applications. In our view, major advantages of nanodisc technology for integral membrane proteins is homogeneity, control of oligomerization state, access to both sides of the membrane, and control of lipids in the local membrane environment of the integral protein. ©2009 by Walter de Gruyter Berlin New York |
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Hamann, Thomas |
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NLEJ248235095 |
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c |
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false |
| hochschulschrift_bool |
false |
| doi_str |
10.1515/BC.2009.091 |
| up_date |
2024-07-06T08:43:45.111Z |
| _version_ |
1803818552643289088 |
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7.4005184 |