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 gram-positive bacterium L. lactis produces the lantibiotic nisin which is a membrane pore forming agent that targets lipid II in other gram-positive organisms. To protect itself from the caustic nature of this lantibiotic, L. lactis produces a protein called NisI which protects itself from the pore-forming agent nisin by binding and inactivating the lantibiotic. We know from previous studies that NisI is disordered when not bound to its cognate substrate nisin. Using spectropolarimetry, we hope to show that NisI becomes ordered upon binding to nisin.
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