ZN-INDUCED PEPTIDE FOLDING

这个子项目是许多研究子项目中利用 资源由NIH/NCRR资助的中心拨款提供。子项目和 调查员(PI)可能从NIH的另一个来源获得了主要资金， 并因此可以在其他清晰的条目中表示。列出的机构是 该中心不一定是调查人员的机构。 对缺乏辅因子的单域蛋白质折叠机制的研究已进入深入阶段，人们开始了解变性后折叠过程中的一系列事件。在某些情况下，甚至可以详细描述所涉及的折叠过渡态和/或中间态的能级、位置和结构。相比之下，关于辅因子诱导的折叠动力学的研究要少得多，尽管大量的蛋白质需要辅因子来实现正确的折叠和/或功能。虽然辅因子结合对不同蛋白质的结构和稳定性的影响可能不同，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的折叠结构。

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.