HELIX-COIL DYNAMICS OF NATURALLY OCCURRING PEPTIDES

天然存在的肽的螺旋线圈动力学

• 批准号: 7955445
• 负责人: DANIEL P RALEIGH
• 金额: $ 0.48万
• 依托单位: UNIVERSITY OF PENNSYLVANIA
• 依托单位国家: 美国
• 财政年份: 2009
• 资助国家: 美国
• 起止时间: 2009-06-01 至 2010-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/7955445
• 关键词: Alanine; Computer Retrieval of Information on Scientific Projects Database; Dependence; Funding; Goals; Grant; Institution; Investigation; Kinetics; Laboratories; Lasers; Light; Modeling; Optics; Peptides; Process; Proteins; Relaxation; Research; Research Personnel; Resources; Role; Sampling; Source; Structure; United States National Institutes of Health; alpha helix; base; design; infrared spectroscopy; insight; protein folding; research study; response

This subproject is one of many research subprojects utilizing the resources provided by a Center grant funded by NIH/NCRR. The subproject and investigator (PI) may have received primary funding from another NIH source, and thus could be represented in other CRISP entries. The institution listed is for the Center, which is not necessarily the institution for the investigator. Helices are not only ubiquitous in proteins, but are also known to sample a wide variety of sequences. However, previous experimental studies on the folding dynamics of monomeric alpha-helices have focused mainly on alanine-based peptides. Since such alanine-rich sequences are rarely encountered in proteins, it is thus imprudent to assume that naturally occurring alpha-helices would show similar folding rates as those of alanine-rich peptides. In light of the important role of secondary structure formation in existing protein folding models, there is a strong need for further investigation of the sequence-dependence of alpha-helix folding kinetics. Herein, we study the relaxation kinetics of a naturally occurring alpha-helix peptide derived from a helical protein as well as a designed helical peptide that is stabilized by salt-bridges, in response to a laser-induced T-jump using infrared (IR) spectroscopy. The goal of this project is to provide further insights into the folding mechanism of alpha-helices and the kinetic role of sidechain-sidechain interactions.

该子项目是利用该技术的众多研究子项目之一 资源由 NIH/NCRR 资助的中心拨款提供。子项目和 研究者 (PI) 可能已从 NIH 的另一个来源获得主要资金， 因此可以在其他 CRISP 条目中表示。列出的机构是 对于中心来说，它不一定是研究者的机构。 螺旋不仅在蛋白质中普遍存在，而且还可以对多种序列进行采样。然而，之前关于单体α螺旋折叠动力学的实验研究主要集中在基于丙氨酸的肽上。由于这种富含丙氨酸的序列在蛋白质中很少遇到，因此假设天然存在的α螺旋将显示与富含丙氨酸的肽相似的折叠率是不明智的。鉴于二级结构形成在现有蛋白质折叠模型中的重要作用，强烈需要进一步研究α螺旋折叠动力学的序列依赖性。 在此，我们研究了源自螺旋蛋白的天然 α 螺旋肽以及通过盐桥稳定的设计螺旋肽的弛豫动力学，以响应使用红外 (IR) 光谱的激光诱导 T 跳跃。该项目的目标是进一步深入了解α螺旋的折叠机制和侧链-侧链相互作用的动力学作用。