The Levinson Lab studies the structural and dynamic basis for protein kinase function. We use a diversified range of methods spanning crystallography, magnetic resonance, and ultrafast spectroscopy to dissect the role of kinase conformational dynamics in catalytic function and drug targeting. Our work has revealed the existence of dynamic water networks in kinase active sites that are important for catalytic function, and shown that large-scale conformational changes play a critical role in selective recognition of kinase inhibitor drugs. We have also shown that kinase engagement with different regulatory partners modulates these dynamic effects to alter inhibitor recognition. We aim to leverage these approaches and insights for the design of next-generation cancer therapeutics that modulate kinase allosteric functions by tuning conformational dynamics.