2009 Fiscal Year Final Research Report
Solid-state NMR analysis of membrane protein complexes with 7-transmembrane helices
| Project/Area Number |
19370068
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biophysics
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| Research Institution | Osaka University |
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Principal Investigator |
FUJIWARA Toshimichi Osaka University, 蛋白質研究所, 教授 (20242381)
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| Project Period (FY) |
2007 – 2009
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| Keywords | 構造生物学 / 生物物理 / 蛋白質 / 原子・分子物理 / ナノバイオ / 生体分子 |
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| Research Abstract |
Solid-state NMR enables the structural determination of biological molecular complexes in unoriented solids. We verified the usefulness of magic-angle spinning solid-state NMR based on dipolar and J couplings for the structural analysis of ^<13>C uniformly labeled biomolecular complexes. We applied solid-state NMR to halorhodopshin, mastoparan-X and 159-redisue transducer protein pHtrII in lipid bilayers. Solid-state NMR provided the detailed structure of mastoparan-X with membranes by combining NMR constraints with replica exchange molecular dynamics simulation using implicit membrane environment. This method was applied to NMR analysis of larger membrane proteins. ^1H-^<13>C correlations of mobile segments of pHtrII were analyzed.
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