Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy.
Oriented and unoriented M13 coat protein, incorporated into dimyristoyl phosphatidylcholine bilayers, has been studied by (13)C-magic angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy. Rotational resonance experiments provided two distance constraints between Calpha and Candz.dbnd6;O...
| Main Authors: | , , |
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| Format: | Journal article |
| Language: | English |
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2000
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| _version_ | 1826271945160654848 |
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| author | Glaubitz, C Gröbner, G Watts, A |
| author_facet | Glaubitz, C Gröbner, G Watts, A |
| author_sort | Glaubitz, C |
| collection | OXFORD |
| description | Oriented and unoriented M13 coat protein, incorporated into dimyristoyl phosphatidylcholine bilayers, has been studied by (13)C-magic angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy. Rotational resonance experiments provided two distance constraints between Calpha and Candz.dbnd6;O positions of the labelled residues Val-29/Val-30 (0.4+/-0.5nm) and Val-29/Val-31 (0.45+/-0. 5nm) in its hydrophobic domain. The derived dihedral angles (Phi, Psi) for Val-30 revealed a local alpha-helical conformation. (13)C-CP-MAS experiments on uniformly aligned samples (MAOSS experiments) using the (13)Candz.dbnd6;O labelled site of Val-30 allowed the determination of the helix tilt (20 degrees +/-10 degrees ) in the membrane. It is shown that one uniform MAS high-resolution solid state NMR approach can be used to obtain structural and orientational data. |
| first_indexed | 2024-03-06T22:04:44Z |
| format | Journal article |
| id | oxford-uuid:4fc2337c-2805-45bf-9dc5-603fbee112fc |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T22:04:44Z |
| publishDate | 2000 |
| record_format | dspace |
| spelling | oxford-uuid:4fc2337c-2805-45bf-9dc5-603fbee112fc2022-03-26T16:09:22ZStructural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4fc2337c-2805-45bf-9dc5-603fbee112fcEnglishSymplectic Elements at Oxford2000Glaubitz, CGröbner, GWatts, AOriented and unoriented M13 coat protein, incorporated into dimyristoyl phosphatidylcholine bilayers, has been studied by (13)C-magic angle spinning nuclear magnetic resonance (MAS NMR) spectroscopy. Rotational resonance experiments provided two distance constraints between Calpha and Candz.dbnd6;O positions of the labelled residues Val-29/Val-30 (0.4+/-0.5nm) and Val-29/Val-31 (0.45+/-0. 5nm) in its hydrophobic domain. The derived dihedral angles (Phi, Psi) for Val-30 revealed a local alpha-helical conformation. (13)C-CP-MAS experiments on uniformly aligned samples (MAOSS experiments) using the (13)Candz.dbnd6;O labelled site of Val-30 allowed the determination of the helix tilt (20 degrees +/-10 degrees ) in the membrane. It is shown that one uniform MAS high-resolution solid state NMR approach can be used to obtain structural and orientational data. |
| spellingShingle | Glaubitz, C Gröbner, G Watts, A Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy. |
| title | Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy. |
| title_full | Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy. |
| title_fullStr | Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy. |
| title_full_unstemmed | Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy. |
| title_short | Structural and orientational information of the membrane embedded M13 coat protein by (13)C-MAS NMR spectroscopy. |
| title_sort | structural and orientational information of the membrane embedded m13 coat protein by 13 c mas nmr spectroscopy |
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