| Project/Area Number |
02650657
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| Research Category |
Grant-in-Aid for General Scientific Research (C)
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| Allocation Type | Single-year Grants |
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| Research Field |
高分子合成
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| Research Institution | Hokkaido University |
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Principal Investigator |
NISHI Norio Department of Polymer Science, Faculty of Science, Hokkaido University, Lecturer, 理学部, 講師 (70001857)
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| Co-Investigator(Kenkyū-buntansha) |
TSUTSUMI Akihiro Department of Applied Physics, Faculty of Engineering, Hokkaido University, Prof, 工学部, 教授 (80000884)
TOKURA Seiichi Department of Polymer Science, Faculty of Science, Hokkaido University, Professo, 理学部, 教授 (40000806)
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| Project Period (FY) |
1990 – 1991
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| Project Status |
Completed (Fiscal Year 1991)
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| Budget Amount *help |
¥2,200,000 (Direct Cost: ¥2,200,000)
Fiscal Year 1991: ¥500,000 (Direct Cost: ¥500,000)
Fiscal Year 1990: ¥1,700,000 (Direct Cost: ¥1,700,000)
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| Keywords | Protein function / Simulation by synthetic chemistry / DNA-binding protein / Protamine / RNA polymerase / Amino acid sequence / Conformation / Turn structure / 蛋白質類似物質(プロテノイド) / RNAポリメラ-ゼII |
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| Research Abstract |
Simulation of protein function by synLheLic chemistry was carried out for DNA-binding proteins such as protamine and RNA polymerase II.
1. Protamines are strongly basic proteins which exist as nucleoprotamines in mature sperm nuclei of fish. Protamines bind strongly to UNA, and play an important functional role in protection of genetic information. however, their DNA-binding mode is unclear so far.
(1)Three kinds of peptides, which emphasized or canceled out the characteristics of the amino acid sequence of turn structure portion in protamine molecules, were synthesized.
(2)Conformation of the above, -three peptides were investigated by CD and ^1H NMR. Their interaction with DNA such as DNA-stabilizing ability and DNA-aggregating ability was also investigated.
(3)An unique sequence, -SRPV-, exists very coservalively in many protamine molecules, and this part is estimated as turn structure portion in the molecule. Three peptide containing this sequence, i. e. SRPV, SSRPV and SSSRPV, were synthesized.
(4)Conformation of the above three peptides were investigated by CD and ^1H NMR.
By the above mentioned approaches, some informations about the conformation and role of the turn structure portion in the protamine molecule were obtained.
2. A repeated sequence of SPTSPSY exists in RNA polymerase II molecule, and the role of this part is unknown. Poly(SPTSPSY)was synthesized as a model for this part. ExacL conformational investigation and interaction with DNA are now in progress.
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