DENATURANT INDUCED EXPANSION AND COMPACTION OF A MULTI-DOMAIN PROTEIN

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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).