Ronald Venters
Assistant Professor in Radiology

I am Director of the Duke University NMR Center and a faculty member in the Duke Radiology Department ( I have over 35 years of experience in the structure determination and dynamics of large biological macromolecules and in NMR methods development.  I am actively involved with training investigators in these areas and in assisting them with their projects.

Current Research Interests

My research program is aimed at determining the structure, dynamics and function of important proteins and protein complexes using high-resolution Nuclear Magnetic Resonance Spectroscopy. My early work as an independent researcher focused on developing NMR experiments and isotopic labeling strategies aimed at studying the structure, dynamics and function of relatively large proteins. This was driven by my desire to extend the field of NMR structure determination to proteins over 20 kDa. Throughout my career I have continued my efforts into advancements of NMR methodologies by writing experiments and analysis tools for the use of Residual Dipolar Couplings as an alternate restraint in structure calculations and in developing fast data collection experiments and spectral reconstruction techniques which save valuable instrument time. My development of new NMR methodologies has always been motivated by the desire to uncover new data on proteins and their functions.

I am currently involved with two major research efforts. I have an ongoing project with a multi-PI RO1 team aimed at developing anti-fungal inhibitors. We have made significant advances towards the goal of developing a fungal specific, non-immunosuppressive calcineurin inhibitors and have published five peer reviewed journal articles over the past few years.

My other collaborative effort is with Perry Blackshear’s group at NIEHS/Duke Biochemistry.  As part of this collaboration, I have generated and analyzed NMR-based structural and dynamics data which continues to offer significant insights regarding RNA binding to the tandem zinc finger motif in Spikemoss (Selaginella moellendorffii). These studies shed light on the mechanistic details of mRNA recognition and binding, key steps that are required to initiate mRNA turnover promoted by the tristetraprolin (TTP) family of RNA binding proteins. 

Current Appointments & Affiliations

Contact Information

  • B127 Lev Sci Res Ctr, #08 Research Drive, Durham, NC 27708
  • Box 3711 Med Ctr, Room B127 Levine Science Research Center, Durham, NC 27710
  • uri icon NMR Center Website

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