Relationship between Conformation and Primary Structure of Cyclic Tetrahpeptides
| Project/Area Number |
60470030
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| Research Category |
Grant-in-Aid for General Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Research Field |
天然物有機化学
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| Research Institution | Kyushu University |
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Principal Investigator |
KATO Tetsuo Kyushu University, 理学部, 助教授 (20037188)
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| Co-Investigator(Kenkyū-buntansha) |
WAKI Michinori Kyushu University, 理学部, 助手 (30037212)
AOYAGI Haruhiko Kyushu University, 理学部, 助手 (80037267)
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| Project Period (FY) |
1985 – 1986
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| Project Status |
Completed (Fiscal Year 1986)
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| Budget Amount *help |
¥6,800,000 (Direct Cost: ¥6,800,000)
Fiscal Year 1986: ¥900,000 (Direct Cost: ¥900,000)
Fiscal Year 1985: ¥5,900,000 (Direct Cost: ¥5,900,000)
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| Keywords | Conformation / Cyclicpeptide / Energy Calculation / エネルギー計算 |
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| Research Abstract |
A useful set of empirical rules is put forward to predict the conformations of cyclic tetrapeptides and cyclic tetradepsipeptides on the basis of primary structure, briefly presented as follows: 1. A conformation allowing an intramolecular hydrogen bond of <gamma> -turn is preferred, and an ester bond always adopts a trans form. 2. On a right-handed peptide ring, the carbonyl group acylating a D residue is oriented to the upper side of the main ring. 3. The carbonyl group acylating a D-proline or an N-methyl-D-amino acid residue is oriented to the lower side of the ring, forming a cis bond. 4. The LDDL configurational sequence adopts a cis-trans-cis-trans backbone with <C_i> symmetry. 5. A glycine residue behaves as a D residue in an L-peptide. Almost all conformations of cyclic tetrapeptides are predicted by these rules. Energetical rationalization of the rules and prediction of possible new conformations are described.
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Report
(1 results)
Research Products
(10 results)
