Shake, Rattle & Roll — the chemistry of RNR proteins

Cathy L. Drennan, Ph.D., of the Massachusetts Institute of Technology and Howard Hughes Medical Institute, will discuss how ribonucleotide reductases (RNRs) shake, rattle and roll to accomplish their critical cellular function, for Albright College’s annual Donald Reinhold chemistry lecture.
The presentation “Shake, Rattle & Roll: Capturing Snapshots of Metalloproteins in Action,” will be held in Klein Hall, Wednesday, April 10, at 7:30 p.m.
What are Metalloproteins?
Metalloproteins utilize metals to perform their functions, and are responsible for a wide range of activities such as the conversion of greenhouse gas carbon dioxide into cellular biomass. To carry out their functions, these proteins often need to be flexible and assume different conformational states, with units of the protein swinging back and forth to enable reactants to bind the protein or products to leave. RNRs are metalloenzymes that convert ribonucleotides (the building blocks of RNA) to deoxyribonucleotides (the building blocks of DNA). RNRs have been targeted for cancer chemotherapies and proposed as candidates for antimicrobial therapies.
The Donald F. Reinhold, Ph.D. ’44 Memorial Chemistry and Biochemistry Lecture
Donald F. Reinhold was born in Reading, raised in South Temple, and graduated from Albright College with a chemistry degree in December 1943. After serving in World War II with the Rainbow Division and earning his doctorate from Rutgers University, Reinhold became a process research chemist with Merck. Over a 38 year pharmaceutical research career, he co-authored 38 patents and played a leading role in the invention and process development of many Merck major products.
This annual lecture in Reinhold’s name brings together current researchers and practitioners to inform and educate creative, curious Albright students and the greater science community.

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