The correct intracellular targeting of protein kinases and phosphatases confers specificity to the enzymes, in part, by placing them in close proximity to their preferred substrates. In addition, the targeting of the enzymes may alter the activity of the protein as structure and dynamics are intimately linked with biological activity. Understanding the physical basis for this activity requires knowledge of the properties of the protein in its native environment, in various free and bound states. Conformational changes may result from subtle movements, such as the rotation of a peptide bond, from gross fluctuations, such as the folding of the protein, or from changes in the relative orientation of domains with respect to one another in a multiprotein complex. The goals for the NMR Core in the next granting period are to: I Provide continued support for high-resolution multinuclear NMR methods and Provide training and expertise for sample preparation and analysis of membrane associated proteins and domains with a combination of solution and solid-state NMR methods.
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