2004 Fiscal Year Final Research Report Summary
Structures and Functions of Membrane Antenna Proteins with High Resolution Solution and Solid State NMR
| Project/Area Number |
15350096
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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 |
Chemistry related to living body
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| Research Institution | Tohoku University |
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Principal Investigator |
NOZAWA Tsunenori TOHOKU UNIVERSITY, Graduate School of Engineering, professor, 大学院・工学研究科, 教授 (10006322)
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| Co-Investigator(Kenkyū-buntansha) |
WANG Zheng-Yu TOHOKU UNIVERSITY, Graduate School of Engineering, Associate Professor, 大学院・工学研究科, 助教授 (10213612)
KBAYASHI Masayuki TOHOKU UNIVERSITY, Graduate School of Engineering, Research Associate, 大学院・工学研究科, 助手 (70271864)
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| Project Period (FY) |
2003 – 2004
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| Keywords | Solution NMR / Solid state high resolution NMR / Photosynthetic antenna complex / LH1(13870) / Chlorosome antenna / BCh1 a / BCh1 c / B820 |
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| Research Abstract |
Main object of the research is to establish the method to elucidate structures and functions of membrane proteins and pigment complexes in terms of high resolution solution nuclear magnetic resonance in conjunction with solid state NMR. For the target of the studies we have selected one of the bacterial membrane antenna, and chlorosome anntena. The membrane antenna called LH1 (light harvesting complex 1) or B870 has subunits (B820) composed of two (α and β) polypeptides and two bacteriochlorophyll molecultes in the active site as the prothetic groups. We have established the methods to elucidate the structures around the prothetic group with use of selectively isotope enriched samples. Thus, we reconstituted the subunit B820 of the LH1 with the isotope enrichied BCh1 a and the normal subumits, or the isotope enriched a and the natural β subunit and the natural BChl a and could resolve the structures with use these samples by the solution NMR. In this case the ^<13>C enriched pigment bacteriochlorophylls and the ^2H enriched proteins could focus the signal of the bacteriochlorophylls and the environment. Futhermore we have make extensive use of multidimensional NMR with these samples. These studies have disclosed the method to elucidate membrane proteins in terms of NMR. The whole unit of LH1, i.e., B870 is too large to be investigated by the solution NMR, we have tried to observe the NMR in full use of solid high resolution NMR. The obtained data have been analyzed in terms of the knowledge of the solution NMR. The assigned signal tells us the B870 would be composed of the subunits with similar structures in the solution states. The multi-dimensional solution NMR and the isotope enrichment have afforded the method to clarify the structure of the component a and R polypeptide in the chloroform/methanol solution
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Research Products
(12 results)
