Latham Lab at UMN

Nuclear magnetic resonance (NMR) spectroscopy is a technique to study the structure and motions of molecules. Solution state biomolecular NMR focuses these methods on the molecules that are important for life and has been used to derive the structures of many important proteins, nucleic acids (DNA and RNA), and multi-subunit complexes.

Structural biology combines biophysics, biochemistry, and molecular biology to study the molecular structure of biological macromolecules. Its particular goals are to determine how proteins and nucleic acids acquire the structures they have and how alterations in their structures affect their function.

Proteins are not strictly static objects, but can populate ensembles of conformations in solution. Transitions between these states occur on a variety of length and time scales, and have been linked to functionally relevant processes such as allosteric signaling and enzyme catalysis. Solution state NMR is uniquely suited to detect and measure these dynamics.

We use sophisticated NMR techniques to probe changes in protein structure and dynamics that occur as part of the functional cycle of large protein-nucleic acid complexes. We couple this information with biochemical assays and in cell experiments, which report on function. By studying wild type and mutants proteins, we obtain a framework for understanding how changes in structure and dynamics choreograph specific macromolecular functions.