Office Address
5-136 Nils Hasselmo Hall
312 Church Street
Minneapolis, MN 55455
United States
Michael Latham
Associate Professor
Biochemistry, Molecular Biology, and Biophysics
Our research program focuses on understanding the interplay of protein structure, dynamics, and function, particularly in large macromolecular assemblies. To accomplish our goals, we utilize sophisticated solution-state NMR spectroscopy techniques, which allow us to probe changes in protein structure and dynamics that occur as part of the functional cycle of the complex. We couple this information with biochemical activity assays and in cell experiments, which report on function. Together, these data will provide a framework for understanding how changes in structure and dynamics of a protein complex choreograph complex functions.
Mission statement
Proteins are the molecular machines that perform the majority of cellular functions. Most proteins work by moving and changing shape in precise ways. Our lab studies how these motions help proteins, especially those in large protein assemblies, do their jobs and perform complex tasks.
We use a technique called NMR spectroscopy to observe proteins in action, along with experiments that test how well they function. By connecting protein movements to their roles in the cell, we aim to understand how life works at the molecular level and what goes wrong in disease.
Research statement
Our laboratory investigates the molecular mechanisms by which protein structure and dynamics enable biological function, with a particular focus on large macromolecular assemblies. We employ advanced solution-state NMR spectroscopy to characterize structural and dynamic changes that occur during the functional cycles of these complexes, which provides residue-specific insights into conformational equilibria, internal motions, and allosteric transitions.
To bridge molecular-level observations with biological outcomes, we integrate NMR-derived structural and dynamic parameters with functional assays that report directly on enzymatic activity, ligand binding, and regulatory control. This combined strategy enables us to construct mechanistic models that link conformational plasticity to biological output. Ultimately, our work seeks to define general principles by which dynamic structural ensembles orchestrate complex biochemical functions in multi-component systems.