Development of the structure analytical method for protein having difficulty in crystallization by the solid-state NMR
Project/Area Number |
24750014
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Research Category |
Grant-in-Aid for Young Scientists (B)
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Allocation Type | Multi-year Fund |
Research Field |
Physical chemistry
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Research Institution | Kanazawa University |
Principal Investigator |
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Project Period (FY) |
2012-04-01 – 2014-03-31
|
Project Status |
Completed (Fiscal Year 2013)
|
Budget Amount *help |
¥4,420,000 (Direct Cost: ¥3,400,000、Indirect Cost: ¥1,020,000)
Fiscal Year 2013: ¥1,170,000 (Direct Cost: ¥900,000、Indirect Cost: ¥270,000)
Fiscal Year 2012: ¥3,250,000 (Direct Cost: ¥2,500,000、Indirect Cost: ¥750,000)
|
Keywords | 分子構造 / 固体NMR / タンパク質 / 原子核間距離 / 立体構造解析 |
Research Abstract |
In this study, the distances between two carbon nuclei in amino acids were estimated from time-dependence of signals recorded by measurements of two-dimensional exchange solid-state nuclear magnetic resonance. We analyzed two amino acids (l-Leucine, l-Alanine) which were labeled two carbon nuclei with carbon-13. We succeeded to estimate the distance between the two carbons of methine and methyl groups in l-Alanine from 0.9 to 1.6 angstroms. Although it was estimated that the distance between carbon nuclei of methine and carboxyl groups in l-Leucine was less than 1.6 angstroms, we could not estimate the lower limit of the distance of l-Leucine. From the above, it is indicated that ranges of distances among carbon nuclei directly-bonding hydrogen nuclei are possibly estimated.
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Report
(3 results)
Research Products
(4 results)