| 磷酰化对丙氨酸与溶菌酶相互作用的影响 |
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| 引用本文： | 方美娟,骆书娜,王河清,刘万云,赵玉芬.磷酰化对丙氨酸与溶菌酶相互作用的影响[J].物理化学学报,2005,21(9):1042-1045. |
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| 作者姓名： | 方美娟 骆书娜 王河清 刘万云 赵玉芬 |
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| 作者单位： | The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry and Engineering, Xiamen University, Xiamen 361005； State Bioorganic Phosphorus Chemistry Laboratory of Education Ministry at Tsinghua University, Department of Life Sciences and Engineering, Tsinghua University, Beijing 100084 |
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| 基金项目： | 福建省科技基金(2001F008)，福建省重点科技基金(2002H011)资助项目~~ |
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| 摘 要： | 在电喷雾离子阱质谱图中发现丙氨酸不能和溶菌酶形成二聚体, 而磷酰化丙氨酸(DIPP-Ala)能和溶菌酶形成二聚体. 进一步研究发现丙氨酸及其他氨基酸磷酰化后, 自身形成二聚能力大大增强. 在Silicon Graplics图形工作站上采用SYBYL 6.8软件, 利用Tripos力场和分子力学方法研究了DIPP-Ala最低能量构象, 并用分子对接(DOCK)研究了二聚体的形成. 结果说明磷氧双键的存在增强了分子间的相互作用.
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| 关 键 词： | ESI-MS 分子间氢键 分子动力学模拟 |
| 收稿时间： | 2005-01-14 |
| 修稿时间： | 2005-04-17 |
The Effect of Phosphoryl Oxygen on the Intermolecular Action of Alanine and Lysozyme |
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| FANG,Mei-Juan,LUO,Shu-Na,WANG,He-Qing,LIU,Wan-Yun,ZHAO,Yu-Fen.The Effect of Phosphoryl Oxygen on the Intermolecular Action of Alanine and Lysozyme[J].Acta Physico-Chimica Sinica,2005,21(9):1042-1045. |
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| Authors: | FANG Mei-Juan LUO Shu-Na WANG He-Qing LIU Wan-Yun ZHAO Yu-Fen |
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| Institution: | The Key Laboratory for Chemical Biology of Fujian Province, Department of Chemistry and Engineering, Xiamen University, Xiamen 361005； State Bioorganic Phosphorus Chemistry Laboratory of Education Ministry at Tsinghua University, Department of Life Sciences and Engineering, Tsinghua University, Beijing 100084 |
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| Abstract: | It was found that N-diisopropyloxyphosphoryl alanine (DIPP-Ala) could form adduct with hen egg white lysozyme (HEWL) as shown in electrospray ionization mass spectroscopy (ESI-MS), but the non-phosphorylated alanine couldn't. The capability for formation of DIPP-Ala dimmer was more stronger than that of alanine. It suggested that a specific non-covalent complex was formed in the solution phase and could be transferred to the gas phase via electrospray ionization (ESI). The results implied that phosphorylated alanine possessed relatively stronger affinities for protein and formed non-covalent complexes with protein more easily than alanine. Using Tripos force field, molecular mechanics calculation on DIPP-Ala dimmer showed that such non-covalent adduct formation was due to the intermolecular hydrogen bond. |
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| Keywords: | ESI-MS Intermolecular hydrogen bond Molecular dynamic simulation |
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