DENATURANT INDUCED EXPANSION AND COMPACTION OF A MULTI-DOMAIN PROTEIN

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。 尽管它在理解蛋白质如何折叠方面具有明显的重要性，但蛋白质的未折叠或变性状态仍然相对未被探索。因此，近年来，越来越多的研究集中在蛋白质在其未折叠状态下的构象特性。特别感兴趣的是那些评估分子尺寸以及构象动力学的蛋白质在各种变性条件下使用合奏或单分子技术。为了验证大的多结构域蛋白质的变性状态是否在化学变性后也表现出类似的行为，我们感兴趣的是用荧光相关光谱（FCS）研究盐酸胍（GdnHCl）诱导的羊抗兔免疫球蛋白G（IgG）的F（ab '）2片段以及IgG结合蛋白A的去折叠。

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. Despite its obvious importance in understanding how proteins fold, the unfolded or denaturated state of proteins remains relatively unexplored. Recent years have thus seen an increasing number of studies focused on the conformational properties of proteins in their unfolded state. Of particular interest are those which assess the molecular dimensions as well as conformational dynamics of proteins under various denaturating conditions using ensemble or single molecule techniques. To verify whether the denaturated states of large multi-domain proteins also exhibit similar behaviors upon chemical denaturation, we are interested to study the guanidine hydrochloride (GdnHCl) induced unfolding of the F(ab')2 fragment of goat anti-rabbit immunoglobulin G (IgG) and also and IgG binding protein, protein A, using fluorescence correlation spectroscopy (FCS).