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 using H/D exchange to map the conformational changes in NikR, an E. coli nikel binding Nik operon repressor. We observe significant differences between the H/D exchange kinetics of NikR binding to various divalent metal ions and are investigating the regions of stabilization as a result of correct binding to Ni2+. Later work will establish the DNA binding site and cooperativity between the monomers in the protein tetramer.
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