ELEMENTARY STEPS OF CHAPERONIN PROMOTED PROTEIN FOLDING

伴侣蛋白促进蛋白质折叠的基本步骤

• 批准号: 2910125
• 负责人: Edward Eisenstein
• 金额: $ 17.54万
• 依托单位: UNIVERSITY OF MD BIOTECHNOLOGY INSTITUTE
• 依托单位国家: 美国
• 财政年份: 1993
• 资助国家: 美国
• 起止时间: 1993-05-01 至 2001-04-30
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2910125
• 关键词: X ray crystallography; adenosine diphosphate; adenosine triphosphate; chemical binding; chemical kinetics; conformation; molecular chaperones; protein folding; site directed mutagenesis

DESCRIPTION: This is an application to continue support in years 4-8 for studies aimed at defining the mechanisms by which the molecular chaperone, GroEL, can assist the folding of denatured proteins. All of the research is to elucidate elementary steps of a single cycle of chaperonin facilitated protein folding. Many different experimental techniques are proposed ranging from site directed mutagenesis to X-ray crystallography and neutron scattering. The use of surface plasmon resonance is well used in these experiments. The proposed research would test 3 specific aims: 1) evaluate predictions of a model for GroEL function based on nucleotide promoted release of polypeptide chains. For example, the use of single-ring variants of GroEL would test the prediction that the ring with bound polypeptide binds nucleotides weakly, but promotes rapid non-native chain release. Further, it will be determined whether full nucleotide occupancy of a single ring is required for release of non-native chains. Methods would include hydrodynamic and scattering studies to determine nucleotide promoted conformational changes and whether they are concerted and follow saturation with nucleotide.

描述：这是一个在4-8年内继续支持的应用程序 研究旨在确定分子 分子伴侣GroEL可以帮助变性蛋白质的折叠。 所有 这项研究是为了阐明一个周期的基本步骤， 伴侣蛋白促进蛋白质折叠。 许多不同的实验 提出了从定点诱变到X射线 晶体学和中子散射。 使用表面等离子体 在这些实验中很好地使用了共振。 拟议研究 将测试3个具体目标：1）评估GroEL模型的预测 基于核苷酸促进多肽链释放的功能。 例如，使用GroEL的单环变体将测试 预测具有结合多肽的环与核苷酸的结合较弱， 但促进快速的非天然链释放。 此外，它将 确定单个环的完整核苷酸占有率是否为 释放非原生链所需的。 方法包括 流体动力学和散射研究，以确定核苷酸促进 构象变化以及它们是否协调一致并遵循 用核苷酸饱和。

项目成果

A monomeric variant of GroEL binds nucleotides but is inactive as a molecular chaperone.

GroEL 的单体变体可结合核苷酸，但作为分子伴侣没有活性。

• DOI: 10.1074/jbc.270.35.20404
• 发表时间: 1995
• 期刊: The Journal of biological chemistry
• 作者: White,ZW;Fisher,KE;Eisenstein,E
• 通讯作者: Eisenstein,E

Nucleotide binding-promoted conformational changes release a nonnative polypeptide from the Escherichia coli chaperonin GroEL.

核苷酸结合促进的构象变化从大肠杆菌伴侣蛋白 GroEL 中释放出非天然多肽。

• DOI: 10.1073/pnas.93.5.1977
• 发表时间: 1996
• 期刊: Proceedings of the National Academy of Sciences of the United States of America
• 影响因子: 11.1
• 作者: Lin,Z;Eisenstein,E
• 通讯作者: Eisenstein,E