Flexibility of membrane proteins by broad-line proton magnetic resonance
| ISSN: |
0005-2736
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|---|---|
| Keywords: |
Dimyristoylphosphatidylcholine ; Membrane protein ; Membrane reconstitution ; Rhodopsin ; ^1H-NMR
|
| Source: |
Elsevier Journal Backfiles on ScienceDirect 1907 - 2002
|
| Topics: |
Biology
Chemistry and Pharmacology
Medicine
Physics
|
| Type of Medium: |
Electronic Resource
|
| URL: |
| _version_ | 1798292206146027520 |
|---|---|
| autor | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. |
| autorsonst | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. |
| book_url | http://linkinghub.elsevier.com/retrieve/pii/0005-2736(83)90519-9 |
| datenlieferant | nat_lic_papers |
| fussnote | Broad-line ^1H-NMR studies of reconstituted membranes of bovine rhodopsin and dimyristoylphosphatidylcholine have demonstrated that the rhodopsin undergoes a considerable increase in motion when the proportion of phospholipid is increased from a small amount (12:1 molar ratio) insufficient to surround the protein completely to a large amount (150:1) which suspends the protein in a bilayer. |
| hauptsatz | hsatz_simple |
| identnr | NLZ18583017X |
| issn | 0005-2736 |
| journal_name | Biochimica et Biophysica Acta (BBA)/Biomembranes |
| materialart | 1 |
| package_name | Elsevier |
| publikationsort | Amsterdam |
| publisher | Elsevier |
| reference | 728 (1983), S. 460-462 |
| schlagwort | Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR |
| search_space | articles |
| shingle_author_1 | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. |
| shingle_author_2 | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. |
| shingle_author_3 | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. |
| shingle_author_4 | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. |
| shingle_catch_all_1 | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. Flexibility of membrane proteins by broad-line proton magnetic resonance Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR 0005-2736 00052736 Elsevier |
| shingle_catch_all_2 | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. Flexibility of membrane proteins by broad-line proton magnetic resonance Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR 0005-2736 00052736 Elsevier |
| shingle_catch_all_3 | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. Flexibility of membrane proteins by broad-line proton magnetic resonance Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR 0005-2736 00052736 Elsevier |
| shingle_catch_all_4 | MacKay, A.L. Elliott Burnell, E. Bienvenue, A. Devaux, P.F. Bloom, M. Flexibility of membrane proteins by broad-line proton magnetic resonance Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR Dimyristoylphosphatidylcholine Membrane protein Membrane reconstitution Rhodopsin ^1H-NMR 0005-2736 00052736 Elsevier |
| shingle_title_1 | Flexibility of membrane proteins by broad-line proton magnetic resonance |
| shingle_title_2 | Flexibility of membrane proteins by broad-line proton magnetic resonance |
| shingle_title_3 | Flexibility of membrane proteins by broad-line proton magnetic resonance |
| shingle_title_4 | Flexibility of membrane proteins by broad-line proton magnetic resonance |
| sigel_instance_filter | dkfz geomar wilbert ipn albert fhp |
| source_archive | Elsevier Journal Backfiles on ScienceDirect 1907 - 2002 |
| timestamp | 2024-05-06T08:44:50.065Z |
| titel | Flexibility of membrane proteins by broad-line proton magnetic resonance |
| titel_suche | Flexibility of membrane proteins by broad-line proton magnetic resonance Broad-line ^1H-NMR studies of reconstituted membranes of bovine rhodopsin and dimyristoylphosphatidylcholine have demonstrated that the rhodopsin undergoes a considerable increase in motion when the proportion of phospholipid is increased from a small amount (12:1 molar ratio) insufficient to surround the protein completely to a large amount (150:1) which suspends the protein in a bilayer. |
| topic | W V WW-YZ U |
| uid | nat_lic_papers_NLZ18583017X |