ZN-INDUCED PEPTIDE FOLDING

锌诱导的肽折叠

• 批准号: 7955441
• 负责人: JEFFERY G SAVEN
• 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/7955441
• 关键词: Binding; Computer Retrieval of Information on Scientific Projects Database; Event; Funding; Grant; Institution; Kinetics; Laboratories; Optics; Peptides; Positioning Attribute; Process; Proteins; Research; Research Personnel; Resources; Source; Staging; Structure; Tertiary Protein Structure; United States National Institutes of Health; cofactor; numb protein; polypeptide

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. The study of the folding mechanism of single domain proteins that lack cofactors has reached an advanced stage wherein the sequence of events along the course of refolding after denaturation begins to be understood. In several cases, it has been even possible to describe in detail the energetics, position, and structure of the folding transition states and/or intermediate states involved. In contrast, there are far fewer studies on cofactor-induced folding kinetics, even though a large number of proteins require cofactors for proper folding and/or function. While the effect of cofactor-binding on the structure and stability may differ for different proteins, many polypeptides can only attain a well-folded structure when associated with their respective cofactors.

这个子项目是许多研究子项目中的一个 由NIH/NCRR资助的中心赠款提供的资源。子项目和 研究者（PI）可能从另一个NIH来源获得了主要资金， 因此可以在其他CRISP条目中表示。所列机构为 研究中心，而研究中心不一定是研究者所在的机构。 缺乏辅因子的单结构域蛋白质的折叠机制的研究已经达到了一个高级阶段，其中沿着变性后重折叠过程的事件顺序沿着开始被理解。在某些情况下，甚至可以详细描述所涉及的折叠过渡态和/或中间态的能量、位置和结构。相比之下，辅因子诱导的折叠动力学的研究要少得多，即使大量的蛋白质需要辅因子进行适当的折叠和/或功能。虽然辅因子结合对结构和稳定性的影响对于不同的蛋白质可能不同，但许多多肽只有在与它们各自的辅因子结合时才能获得良好折叠的结构。