Visualizing Enzymes in Action

Molecular motions play an important role in the regulation and function of enzymes, nature’s catalysts. What are the structural dynamics involved in protein allostery and catalysis? How do flexible enzymes perform challenging chemistry? Can we animate crystal structures of proteins? These are outstanding questions in biology, which motivate studies of proteins in motion. Capturing proteins in action is the next frontier of structural biology.

Nozomi Ando, Chemistry and Chemical Biology, is using new x-ray methods to visualize how proteins tune their activities and perform sequential reactions in the correct order. Ando is working at the interface of biochemistry and physical chemistry. She aims to go beyond the static picture of enzymes obtained by traditional Bragg diffraction and instead recover dynamic information with non-conventional x-ray scattering approaches.

Ando’s lab is particularly interested in enzymes of biomedical importance, and which have been challenging to study using traditional methods. This includes enzymes that could be used as drug targets, as well as enzymes with complex mechanisms to synthesize natural products with pharmaceutical potential.

NIH Award Number: 7R35GM124847-02

Cornell Researchers

Funding Received

$1.5 Million spanning 4 years