MPS seminar J. Patrick Loria

Biophysical characterization of enzyme motions: From A to Z.

Solution NMR experiments were used to address the role of protein motions in catalytic function in three enzymes ranging in size from 13 – 66 kDa. In ribonuclease A and triosephosphate isomerase, these experiments identified ms – ms loop motions in regions at and distant from the active that are important for enzyme motions. In both systems mutagenesis, loop swapping, and enzymatic assays support the role of coupled motions between loops as an integral component of enzyme activity. In ribonuclease Z, solution NMR experiments identified large conformational changes that must occur before, or simultaneous to, substrate binding in order for catalysis to occur. In all cases solution NMR has documented previously unappreciated roles of protein motion in enzymatic function.

 

Dec 19 2008, 14:00 sal B: J. Patrick Loria, Yale University.

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