AnaIysis of dynamic behavior of ribonuclease upon ligand binding using high resolution NMR
使用高分辨率 NMR 分析配体结合时核糖核酸酶的动态行为
基本信息
- 批准号:12672088
- 负责人:
- 金额:$ 2.56万
- 依托单位:
- 依托单位国家:日本
- 项目类别:Grant-in-Aid for Scientific Research (C)
- 财政年份:2000
- 资助国家:日本
- 起止时间:2000 至 2001
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
The idea that the internal motions in enzymes were restricted upon ligand binding has been accepted. Recently, it was reported that internal motions in some enzymes such 4-oxalocrotonate tautomerase, hen and human lysozymes increased upon ligand binding. Now, it is controversial whether internal motions in enzymes increase or not upon ligand binding. Therefore, in this research, in order elucidate whether the increased internal motions in enzymes upon binding its ligand is in general or not, we prepared ^<15>N uniformly labeled ribonuclease T1 from Pichia pastoris and measured the relaxation time (T_1 and T_2) of nitrogen atoms and NOEs between ^1H and ^<15>N in them in the presence or absence of 3'-GMP. Order parameters in every residues of ^<15>N uniformly labeled ribonuclease T1 was calculated by model free analysis, of the relaxation time (T_1 and T_2) of nitrogen atoms and NOEs between ^1H and ^<15>N. As the results, it was elucidated that some residues in ribonuclease T1 had the smaller order parameters, indicating that the internal motions in ribonuclease T1 molecule increased upon binding its ligand.
酶的内部运动受配体结合限制的观点已被接受。最近有报道称,一些酶如4-草草酸互变酶、母鸡和人溶菌酶的内部运动在配体结合后增加。目前,酶的内部运动是否在配体结合时增加是有争议的。因此,在本研究中,为了阐明酶结合其配体后增加的内部运动是否具有全局性,我们从毕赤酵母中制备了^<15>N均匀标记的核糖核酸酶T1,并测量了它们在3′-GMP存在或不存在的情况下^1H至^<15>N之间的氮原子弛豫时间(T_1和T_2)和NOEs。通过模型自由分析,计算了均匀标记的核糖核酸酶T1 ^<15>N的每个残基中氮原子弛豫时间(T_1和T_2)和^1H至^<15>N之间NOEs的序参量。结果表明,核糖核酸酶T1中一些残基的序参量更小,说明核糖核酸酶T1分子在与其配体结合后,其内部运动增强。
项目成果
期刊论文数量(13)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
Ohmura T. Ueda T. Ootsuka K. Saito M. Imoto T.: "Stabilization of hen egg white lysozyme by a cavity-filling mutation"Protein Sci.. 10. 313-320 (2001)
Ohmura T. Ueda T. Ootsuka K. Saito M. Imoto T.:“通过空腔填充突变稳定鸡蛋清溶菌酶”Protein Sci.. 10. 313-320 (2001)
- DOI:
- 发表时间:
- 期刊:
- 影响因子:0
- 作者:
- 通讯作者:
UedaT. Nagata M. ImotoT.: "Aggregation and chemical reaction in hen lysozyme caused by heating at pH 6 are depressed by osmolytes, sucrose and trehalose"J. Biochem.. 130. 491-496 (2001)
上田T.
- DOI:
- 发表时间:
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- 影响因子:0
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- 通讯作者:
Ohmura T, Ueda T et al.: "Stabilization of hen egg white Iysozyme by a cavity-filling mutation"Protein Science. 10. 313-320 (2001)
Ohmura T、Ueda T 等人:“通过空腔填充突变稳定鸡蛋清溶菌酶”蛋白质科学。
- DOI:
- 发表时间:
- 期刊:
- 影响因子:0
- 作者:
- 通讯作者:
Obita T, Ueda T et al.: "Assignment of ^1H and ^<15>N resonances of mouse lysozyme M"J. Biomolecular NMR. 18. 361-362 (2000)
Obita T、Ueda T等人:“小鼠溶菌酶M的^1H和^15N共振的分配”J。
- DOI:
- 发表时间:
- 期刊:
- 影响因子:0
- 作者:
- 通讯作者:
Ueda T et al.: "Aggregation and chemical reaction in hen lysozyme caused by heating at pH 6 are depressed by osmolytes, sucrose and trehalose"J. Biochem.. 130. 491-496 (2001)
Ueda T 等人:“渗透剂、蔗糖和海藻糖抑制了在 pH 6 下加热引起的母鸡溶菌酶的聚集和化学反应”J.
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- 影响因子:0
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Establishment of research foundation on "objective pain assessment" using animal models suffering from neuropathic pain
建立使用神经病理性疼痛动物模型进行“客观疼痛评估”的研究基础
- 批准号:
26293129 - 财政年份:2014
- 资助金额:
$ 2.56万 - 项目类别:
Grant-in-Aid for Scientific Research (B)
Development of Fab molecule with the stable scaffold for next generation
开发具有下一代稳定支架的 Fab 分子
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23655160 - 财政年份:2011
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$ 2.56万 - 项目类别:
Grant-in-Aid for Challenging Exploratory Research
Study on the development of molecules for depressing neuropathic pain based on tertiary structure of human P2X4 receptor
基于人P2X4受体三级结构的抑制神经性疼痛分子的开发研究
- 批准号:
23390155 - 财政年份:2011
- 资助金额:
$ 2.56万 - 项目类别:
Grant-in-Aid for Scientific Research (B)
Improved function of ketoamine oxidase for clinical examination reagent of diabetes by use of multiple approaches
多途径提高糖尿病临床检验试剂酮胺氧化酶的功能
- 批准号:
20590579 - 财政年份:2008
- 资助金额:
$ 2.56万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
Analysis on mechanism of severe allergic reaction caused by SNP in interleukin 13 using NMR
NMR分析白细胞介素13中SNP引起严重过敏反应的机制
- 批准号:
14572032 - 财政年份:2002
- 资助金额:
$ 2.56万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
Construction of an effective renaturation method of denatured proteins based on a biological function
基于生物学功能的变性蛋白有效复性方法的构建
- 批准号:
08558072 - 财政年份:1996
- 资助金额:
$ 2.56万 - 项目类别:
Grant-in-Aid for Scientific Research (A)
Analysis of dynamic behavior of mutant hen lysozyme with larger catalytic constant using high resolution NMR
利用高分辨率核磁共振分析具有较大催化常数的突变母鸡溶菌酶的动态行为
- 批准号:
07680725 - 财政年份:1995
- 资助金额:
$ 2.56万 - 项目类别:
Grant-in-Aid for Scientific Research (C)
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