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Solid-state nuclear magnetic resonance studies of enzyme-substrate complexes.
Solid-state NMR (SSNMR) spectroscopy is a powerful technique for studying enzymatic reactions in situ with direct access to the dynamics of the reaction. Micro-crystalline proteins and polypeptide samples and enzyme-inhibitor complexes can be studied by SSNMR directly in the solid state, in solution in H2O, or in the various crystalline environments (powder, thin films, thin slices) that are accessible to common SSNMR spectroscopy. Examples of enzyme-inhibitor complexes studied by solid-state NMR are reported, with a special emphasis on the polypeptide chain dynamics in the binding domain. SSNMR can characterize the conformation and dynamics of the complex in the solid state. Moreover, it can be used to probe weak interactions and highly transient states of the protein. The dynamics of the substrate in the active site, the early stages of the reaction, and the role of the active site environment may be probed by SSNMR. The research on enzyme dynamics described in this article may help to establish a link between protein structure and function, and how dynamics changes with active site binding. UNPUBLISHED
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