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. We are continuing the development of a protocol for H/D exchange of proteins. The protocol is directed at an aspect of protein folding that is not being pursued by others; namely the interaction of proteins with metal ions and with other substances such as proteins, peptides, drugs. An area of particular interest is the conformational changes that occur to calmodulin as it interacts with peptides and with calcium ions in solution. We have improved considerable the methodology for conducting a titration of a protein with a metal ion. We learned in the course of this work that the conformational collapse in calmodulin (which we view as a on/off switch) is maximized when hydrophobic peptides are present during the titration. We are turning the method development (core research) into a collaboration with Dr. M. Shea (University of Iowa), an expert in calmodulin. Dr. Shea is providing calmodulins from other species (paramecium, rat) to complement our work with porcine calmodulin and half calmodulins (half proteins that are expressed to contain only two, rather than four, calcium binding sites). We believe that this method development and application will lead to a new tool in protein chemistry and proteomics.
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