Dynamics of Polypeptide Diffusion and Collapse
多肽扩散和塌陷的动力学
基本信息
- 批准号:0077907
- 负责人:
- 金额:$ 30万
- 依托单位:
- 依托单位国家:美国
- 项目类别:Continuing grant
- 财政年份:2000
- 资助国家:美国
- 起止时间:2000-09-01 至 2004-08-31
- 项目状态:已结题
- 来源:
- 关键词:
项目摘要
HagenMCB 0077907This project will clarify the relationship between landscape and parameter regimes that have been explored in models and simulations of folding, and the properties of real protein molecules. It will use time-resolved laser spectroscopy to probe the conformational dynamics of unfolded and partially folded protein molecules, with the aim of extracting basic parameters of importance to landscape descriptions of folding. Laser photolysis experiments on unfolded cytochrome-c and other molecules will allow measurement of the rate of conformational diffusion of an unfolded polypeptide, the effect of inter-residue interactions on that diffusion, and the limitations that this diffusion places on overall folding speed. They will also allow direct measurement of the time scales on which compact denatured proteins interconvert between differentconfigurations; this time scale directly indicates the degree of 'roughness' in landscape descriptions. Using nanosecond-resolved laser temperature jump spectroscopy, this work will also examine the properties of a protein molecule that determine the dynamics of its collapse - the rapid transition from expanded to compact denatured configurations. These experiments will enhance understanding of dynamical events that occur earlyin protein folding, and they should also provide grounds for more detailed comparisons between protein folding theory and experiment.The question of how proteins fold - how a randomly coiled polypeptide chain attains its proper compact structure - remains one of the most important and interesting problems at the interface of biology, chemistry, and physics. The study of folding has benefited in recent years from several very significant advances in both theory and experimental technique. Theoreticians have developed a "new view", or "energy landscape" description of protein folding, which uses statistical ideas from condensed matter physics to identify and explore those characteristics of proteins that directly control the speed and dynamics of the folding process. At the same time, experimental advances have included the development of new optical methods for triggering and observing the rapid phases of folding, which occur on nanosecond or microsecond time scales. Because these new techniques allow experimentalists to explore and resolve the very earliest events in folding, it is now possible to investigate the connection between real protein molecules and the simplified model proteins studied by theoreticians. Applying new optical techniques, this work aims to strengthen the connection between theory and experiment by characterizing the shapes and statistical properties of energy landscapes of actual molecules, and the dynamics of diffusion on those landscapes.
HagenMCB 0077907该项目将阐明在折叠模型和模拟中探索的景观和参数制度之间的关系,以及真实的蛋白质分子的性质。 它将使用时间分辨激光光谱来探测未折叠和部分折叠的蛋白质分子的构象动力学,目的是提取对折叠的景观描述具有重要意义的基本参数。 对未折叠的细胞色素C和其他分子的激光光解实验将允许测量未折叠多肽的构象扩散速率、残基间相互作用对该扩散的影响以及该扩散对整体折叠速度的限制。 它们还将允许直接测量紧凑的变性蛋白质在不同构型之间相互转换的时间尺度;这个时间尺度直接指示景观描述中的“粗糙度”。 利用纳秒分辨激光温度跃变光谱,这项工作还将研究蛋白质分子的性质,这些性质决定了其崩溃的动力学-从膨胀到紧凑的变性构型的快速转变。 这些实验将增强对蛋白质折叠早期发生的动力学事件的理解,也将为蛋白质折叠理论和实验之间更详细的比较提供基础。蛋白质如何折叠的问题--一条随机卷曲的多肽链如何获得其适当的紧凑结构--仍然是生物学、化学和物理学界面上最重要和最有趣的问题之一。 近年来,折叠的研究得益于理论和实验技术上的几个非常重要的进展。 理论家们已经开发了一种蛋白质折叠的“新观点”或“能量景观”描述,它使用凝聚态物理学的统计思想来识别和探索直接控制折叠过程速度和动力学的蛋白质特征。 与此同时,实验方面的进展包括开发了新的光学方法,用于触发和观察折叠的快速阶段,这些阶段发生在纳秒或微秒的时间尺度上。 由于这些新技术使实验学家能够探索和解决折叠过程中最早的事件,现在有可能研究真实的蛋白质分子与理论家研究的简化模型蛋白质之间的联系。 应用新的光学技术,这项工作旨在通过表征实际分子能量景观的形状和统计特性以及这些景观上的扩散动力学来加强理论与实验之间的联系。
项目成果
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Stephen Hagen其他文献
Cover crops, crop insurance losses, and resilience to extreme weather events
覆盖作物、作物保险损失和应对极端天气事件的能力
- DOI:
10.1111/ajae.12431 - 发表时间:
2023 - 期刊:
- 影响因子:4.2
- 作者:
Serkan Aglasan;R. Rejesus;Stephen Hagen;William Salas - 通讯作者:
William Salas
Stephen Hagen的其他文献
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{{ truncateString('Stephen Hagen', 18)}}的其他基金
Collaborative Research: Evolution of information processing in the Vibrio fischeri pheromone-signaling network
合作研究:费氏弧菌信息素信号网络中信息处理的演变
- 批准号:
1715981 - 财政年份:2017
- 资助金额:
$ 30万 - 项目类别:
Standard Grant
An Advanced Laboratory in Biological Physics
生物物理先进实验室
- 批准号:
1139906 - 财政年份:2012
- 资助金额:
$ 30万 - 项目类别:
Standard Grant
CAREER: Understanding Protein Folding Dynamics in the Ultra-Fast Limit
职业:了解超快极限下的蛋白质折叠动力学
- 批准号:
0347124 - 财政年份:2004
- 资助金额:
$ 30万 - 项目类别:
Continuing grant
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