Molten-Globule of Proteins and Its Physiological Role

蛋白质熔球及其生理作用

基本信息

  • 批准号:
    02454536
  • 负责人:
  • 金额:
    $ 4.48万
  • 依托单位:
  • 依托单位国家:
    日本
  • 项目类别:
    Grant-in-Aid for General Scientific Research (B)
  • 财政年份:
    1990
  • 资助国家:
    日本
  • 起止时间:
    1990 至 1992
  • 项目状态:
    已结题

项目摘要

The molten globule is a compact denatured state with a significant amount of secondary structure, but largely disordered tertiary structure. To understand the role of the molten globule in protein folding and its physiological role, we studied the conformation and stability of the molten globule of various proteins and the corresponding state of peptides. We obtained following major results.1. The stability of the molten globule is determined by a balance of various forces. We showed that electrostatic repulsion is a critical factor destabilizing the molten globule state.2. The molten globule of cytochrome c was studied by small angle X-ray scattering and its conformational properties were clarified.3. We indicated that the reversibly denatured conformation of cytochrome c under physiological conditions (i.e. neutral ph, physiological temperature and no denaturant) is the molten globule.4. We showed the mechanism of the anion and ph-dependent conformational transition of melittin and an amphiphilic polypeptide.5. We showed that Guanidine-Hydrochloride induces the refolding of acid-unfolded proteins, stabilizing the molten globule state.
熔融球是一种致密的变性状态,具有大量的二级结构,但很大程度上是无序的三级结构。为了了解熔融球在蛋白质折叠中的作用及其生理作用,我们研究了各种蛋白质的熔融球的构象和稳定性以及肽的相应状态。取得了以下主要成果:1.熔融球的稳定性取决于各种力的平衡。我们发现静电斥力是使熔融球态不稳定的关键因素.利用小角X射线散射技术研究了细胞色素c熔融球的构象特征.研究表明,在生理条件下(即中性ph、生理温度和无变性剂),细胞色素c的可逆变性构象为熔融球.揭示了蜂毒肽和两亲性多肽构象转变的阴离子和ph依赖性机理.我们发现盐酸胍诱导酸解折叠蛋白质的重折叠,稳定熔融球状态。

项目成果

期刊论文数量(60)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
後藤 祐児,高木 俊夫: "誌上対談 モルテン・グロビュ-ルをめぐって" 蛋白質核酸酵素. 37. 772-780 (1992)
Yuji Goto、Toshio Takagi:“熔球的期刊讨论”蛋白质核酸酶 37. 772-780 (1992)
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    0
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Kataoka,M.,Hagihara,Y., Mihara,K. & Goto,Y: "Molten Globule of Cytochrome c Studied by Small Angle X-Ray Scattering." J. Mol. Biol. 229. 591-596 (1993)
片冈,M.,萩原,Y.,三原,K.
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    0
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Kataoka,H.,Hagihara,Y.,Mihara,K. & Goto,Y.: "Molten Globule of Cytochrome c Studied by Small Angle X-Ray Scattering" J.Mol.Biol.229. 591-596 (1993)
片冈 H.、萩原 Y.、三原 K.
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    0
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Yuji Goto et al.: "Mechanism of AcidーInduced Folding of proteins." Bichemistry. 29. 3480-3488 (1990)
Yuji Goto 等人:“酸诱导的蛋白质折叠机制”。29. 3480-3488 (1990)。
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    0
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Hagihara,Y.,Kataoka,M.,Aimoto,S.& Goto,Y.: "Charge Repulsion in the Conformational Stability of Melittin" Biochemistry. 31. 11908-11914 (1992)
萩原 Y.、片冈 M.、相本 S.
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GOTO Yuji其他文献

The energy spectrum of forward photons measured by the RHICf experiment in $\sqrt{s}$ = 510 GeV proton-proton collisions
$sqrt{s}$ = 510 GeV 质子-质子碰撞中 RHICf 实验测得的前向光子能谱
  • DOI:
    10.22323/1.358.0413
  • 发表时间:
    2019
  • 期刊:
  • 影响因子:
    0
  • 作者:
    Sato Kenta;Itow Yoshitaka;Menjo Hiroaki;Ueno Mana;Ohashi Ken;Sako Takashi;GOTO Yuji;Nakagawa Itaru;Saidl R.;Park Junsang;Kim Minho;Hong Byungsik;Tanida Kiyoshi;Torii Shoji;Kasahara Katsuaki;Sakurai Nobuyuki;Adriani Oscar;D'Alessandro Raffaello;Bonechi Lor
  • 通讯作者:
    Bonechi Lor

GOTO Yuji的其他文献

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{{ truncateString('GOTO Yuji', 18)}}的其他基金

Role of supersaturation in the formation of amyloid fibrils
过饱和在淀粉样原纤维形成中的作用
  • 批准号:
    24370067
  • 财政年份:
    2012
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Development of the polarized target for spin-structure studies of the proton in the FNAL-E906 experiment
开发用于 FNAL-E906 实验中质子自旋结构研究的偏振靶
  • 批准号:
    22340070
  • 财政年份:
    2010
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Chromatin structure and nuclear territories of the intergenic region between inactivated and escape genes on human inactive X chromosome.
人类失活 X 染色体上失活基因和逃逸基因之间基因间区域的染色质结构和核区域。
  • 批准号:
    22770008
  • 财政年份:
    2010
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for Young Scientists (B)
Understanding the amyloid fibril formation of β2-microglobulin on the basis of protein conformation
基于蛋白质构象了解 β2-微球蛋白淀粉样原纤维的形成
  • 批准号:
    13480219
  • 财政年份:
    2001
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B)
Role of α-β transition in the folding of proteins
α-β转变在蛋白质折叠中的作用
  • 批准号:
    11694208
  • 财政年份:
    1999
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B).
Single molecular analysis of protein folding
蛋白质折叠的单分子分析
  • 批准号:
    10480181
  • 财政年份:
    1998
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for Scientific Research (B).
Folding Mechanism of beta-Lactogobulin
β-乳球蛋白的折叠机制
  • 批准号:
    09044221
  • 财政年份:
    1997
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for international Scientific Research
Structure and function of beta2-glycoprotein I
β2-糖蛋白 I 的结构和功能
  • 批准号:
    07680650
  • 财政年份:
    1995
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for Scientific Research (C)
Joint Study on the Mechanism of Protein Folding
蛋白质折叠机制联合研究
  • 批准号:
    07044200
  • 财政年份:
    1995
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for international Scientific Research
Molten Globule State of Proteins-Conformation, Stability, and Its Physiological Role
蛋白质的熔球状态——构象、稳定性及其生理作用
  • 批准号:
    05044131
  • 财政年份:
    1993
  • 资助金额:
    $ 4.48万
  • 项目类别:
    Grant-in-Aid for international Scientific Research

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考虑蛋白质的结构:使用基于图的卷积神经网络预测感染是否对 B-内酰胺抗生素具有耐药性
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蛋白质网络层次结构分析
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