Awardee OrganizationUNIVERSITY OF WISCONSIN-MADISON
Description
Abstract Text
This subproject is one of many research subprojects utilizing the resources
provided by a Center grant funded by NIH/NCRR. Primary support for the subproject
and the subproject's principal investigator may have been provided by other sources,
including other NIH sources. The Total Cost listed for the subproject likely
represents the estimated amount of Center infrastructure utilized by the subproject,
not direct funding provided by the NCRR grant to the subproject or subproject staff.
Thioredoxin proteins are important for maintaining the proper thiol redox state in cells. We are studying thioredoxinsw, and their interactions with thioredoxin reductases, from bacteria that are considered drug targets. To this end, we are determining the 3-dimensional structures of these thioredoxin proteins, and exploring their interactions (binding surfaces) with thioredoxin reductase partners.This, and other protects, are also focused on drug design, and studies of protein-ligand interactions to guide drug design. This involves NMR analysis of protein ligand complexes, including ligands that are designed using "fragment-assembly" techniques that my lab specializes in. Besides characterizing binding interfaces, we are also interested in changes to dynamic state of the protein and ligand, upon binding.
Public Health Relevance Statement
Data not available.
NIH Spending Category
Biotechnology
Project Terms
BacteriaBindingCellsComplexDrug Delivery SystemsDrug DesignFundingGrantLigandsNational Center for Research ResourcesOxidation-ReductionPrincipal InvestigatorProtein AnalysisProteinsResearchResearch InfrastructureResourcesSourceStructureSulfhydryl CompoundsSurfaceTechniquesThioredoxinUnited States National Institutes of Healthcostdesigninterestthioredoxin reductasethree dimensional structure
No Sub Projects information available for 5P41RR002301-26 5405
Publications
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