Vanderbilt Nuclear Magnetic Resonance (NMR)


VICB RESEARCH Nuclear Magnetic Resonance (NMR)
Organic chemists have used NMR for the characterization of small molecules for decades, and the VICB’s Small Molecule NMR Core Facility, under the direction of Don Stec provides state-of-the-art instrumentation and expertise for just that purpose. However, the use of NMR has now expanded to include the characterization of protein and nucleic acid macromolecules. Many VICB members, some in collaboration with the Center for Structural Biology (CSB), use this approach in addition to other spectroscopic methods to study a wide array biomolecular structures and interactions. Steve Fesik uses NMR techniques to detect the binding of small molecules to protein targets as part of his fragment-based approach to drug design. NMR also assists in determining the site of lead molecule binding to the protein of interest. These methods will be a key component in the cancer Drug Discovery Program that is being developed at Vanderbilt under Dr. Fesik’s direction (see Cancer). Walter Chazin uses NMR to probe the structure and dynamics of large proteins and multi-protein machines in order to understand DNA replication, damage response and repair, and calcium and ubiquitination signaling in cells. Chuck Sanders is pushing the envelop for NMR-based protein structure determination and recently solved the structure of the 42 kD diacylglycerol kinase enzyme. The lab will now use their structural data to determine how mutations of the enzyme result in misfolding and lead to aberrant function. Al Beth capitalizes on the ability of EPR (electron paramagnetic resonance) to probe protein structure in solution or in a membrane bilayer. His interest is in the structure and function of the erythrocyte anion exchange protein, and in the epidermal growth factor and serotonin receptors. His studies are focused on understanding the dynamics of each protein upon ligand binding and signal transduction processes. Mike Stone’s primary interest is on nucleic acids rather than proteins. His work has led to increased understanding of the effect of damaged bases on DNA structure and on the interaction of the DNA with replication and/or repair enzymes.
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Organic chemists have used NMR for the characterization of small molecules for decades, and the VICB’s Small Molecule NMR Core Facility, under the direction of Don Stec provides state-of-the-art instrumentation and expertise for just that purpose. However, the use of NMR has now expanded to include the characterization of protein and nucleic acid macromolecules. Many VICB members, some in collaboration with the Center for Structural Biology (CSB), use this approach in addition to other spectroscopic methods to study a wide array biomolecular structures and interactions.

Steve Fesik uses NMR techniques to detect the binding of small molecules to protein targets as part of his fragment-based approach to drug design. NMR also assists in determining the site of lead molecule binding to the protein of interest. These methods will be a key component in the cancer Drug Discovery Program that is being developed at Vanderbilt under Dr. Fesik’s direction (see Cancer).

Walter Chazin uses NMR to probe the structure and dynamics of large proteins and multi-protein machines in order to understand DNA replication, damage response and repair, and calcium and ubiquitination signaling in cells. Chuck Sanders is pushing the envelop for NMR-based protein structure determination and recently solved the structure of the 42 kD diacylglycerol kinase enzyme. The lab will now use their structural data to determine how mutations of the enzyme result in misfolding and lead to aberrant function.

Al Beth capitalizes on the ability of EPR (electron paramagnetic resonance) to probe protein structure in solution or in a membrane bilayer. His interest is in the structure and function of the erythrocyte anion exchange protein, and in the epidermal growth factor and serotonin receptors. His studies are focused on understanding the dynamics of each protein upon ligand binding and signal transduction processes.

Mike Stone’s primary interest is on nucleic acids rather than proteins. His work has led to increased understanding of the effect of damaged bases on DNA structure and on the interaction of the DNA with replication and/or repair enzymes.