MECHANISMS OF CHAPERONIN-ASSISTED PROTEIN FOLDING
伴侣蛋白辅助蛋白质折叠的机制
基本信息
- 批准号:2186892
- 负责人:
- 金额:$ 9.05万
- 依托单位:
- 依托单位国家:美国
- 项目类别:
- 财政年份:1994
- 资助国家:美国
- 起止时间:1994-05-01 至 1999-04-30
- 项目状态:已结题
- 来源:
- 关键词:adenosine diphosphate adenosine triphosphate alpha glucosidase bioenergetics chemical association chemical binding chemical kinetics conformation electron microscopy glutamate ammonia ligase hydrolysis microcalorimetry molecular chaperones nucleotide analog protein folding protein sequence proteolysis solutions stoichiometry stop flow technique thermodynamics thiosulfate sulfurtransferase
项目摘要
A number of in vivo protein folding and assembly reactions have been
found to require an essential set of accessory proteins called
chaperonins. Their mechanism of action is unknown. We will use
dodecameric Escherichia coli glutamine synthetase (GS), mitochondria
rhodanese, and yeast alpha-glucosidase as substrates for the E. coli
chaperonin system, groEL and groES. Rhodanese requires all the
chaperonin components and ATP for folding while GS and a-glucosidase only
require groEL and ATP to initiate folding. Determining the molecular
origins for these observed differences will provide important mechanistic
information about chaperonin-assisted folding and assembly.
The long range goal of our research is to define the mechanism by which
the groE chaperonins increase the product yields of correctly folded
oligomeric and monomeric proteins. The main hypotheses to be tested are
that; 1) GroEL modulates its binding affinity for partially folded
intermediates (PFI) by binding nucleotide (ATP, ADP, ATP analogs) and
groES to rapidly release the previously bound substrate and; 2)the
molecular origins of the different requirements of the chaperonin system
observed with various substrates are dictated by a) nature and strength
of binding of the initial folding intermediate and b) whether the release
intermediate still has a tendency to misfold or aggregate.
Our experimental approach is to; 1) determine the binding enthalpies and
free energies between groEL and nucleotides, groES, and stable folding
intermediates by differential stopped-flow titration microcalorimetry;
2) determine whether the chaperonin system is still required after the
PFI has been released from immobilized (yet functional) groEL; and 3)
determine the kinetics (monitoring time-dependent activity, fluorescence
and enthalpic changes) of chaperonin-assisted folding (and assembly)
reactions as a function of increasing concentrations of stable
chaperonin-PFI complexes.
许多在体内的蛋白质折叠和组装反应已经被发现
项目成果
期刊论文数量(0)
专著数量(0)
科研奖励数量(0)
会议论文数量(0)
专利数量(0)
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Mark T Fisher其他文献
Mark T Fisher的其他文献
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{{ truncateString('Mark T Fisher', 18)}}的其他基金
CryoEM analysis of Anthrax Toxin Pore Complexes
炭疽毒素孔隙复合物的冷冻电镜分析
- 批准号:
8108210 - 财政年份:2011
- 资助金额:
$ 9.05万 - 项目类别:
CryoEM analysis of Anthrax Toxin Pore Complexes
炭疽毒素孔隙复合物的冷冻电镜分析
- 批准号:
8230465 - 财政年份:2011
- 资助金额:
$ 9.05万 - 项目类别:
CryoEM analysis of Anthrax Toxin Pore Complexes
炭疽毒素孔隙复合物的冷冻电镜分析
- 批准号:
8431446 - 财政年份:2011
- 资助金额:
$ 9.05万 - 项目类别:
CryoEM analysis of Anthrax Toxin Pore Complexes
炭疽毒素孔隙复合物的冷冻电镜分析
- 批准号:
8132761 - 财政年份:2010
- 资助金额:
$ 9.05万 - 项目类别:
A Chaperonin/Osmolyte Protein Folding Screen - STTR Phase I
伴侣蛋白/渗透调节蛋白折叠筛选 - STTR 第一阶段
- 批准号:
7221111 - 财政年份:2007
- 资助金额:
$ 9.05万 - 项目类别:
MECHANISMS OF CHAPERONIN-ASSISTED PROTEIN FOLDING
伴侣蛋白辅助蛋白质折叠的机制
- 批准号:
2415198 - 财政年份:1994
- 资助金额:
$ 9.05万 - 项目类别:
MECHANISMS OF CHAPERONIN-ASSISTED PROTEIN FOLDING
伴侣蛋白辅助蛋白质折叠的机制
- 批准号:
2186891 - 财政年份:1994
- 资助金额:
$ 9.05万 - 项目类别:
MECHANISMS OF CHAPERONIN-ASSISTED PROTEIN FOLDING
伴侣蛋白辅助蛋白质折叠的机制
- 批准号:
2701591 - 财政年份:1994
- 资助金额:
$ 9.05万 - 项目类别:
MECHANISMS OF CHAPERONIN-ASSISTED PROTEIN FOLDING
伴侣蛋白辅助蛋白质折叠的机制
- 批准号:
2186893 - 财政年份:1994
- 资助金额:
$ 9.05万 - 项目类别:
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