Probing protein quinary structures by in-cell NMR

International Conference on Histochemistry & Cell Biology

September 14-15, 2016 Phoenix, USA

Alexander Shekhtman

State University of New York, USA

Posters & Accepted Abstracts: J Cytol Histol

Abstract :

Historically introduced by McConkey to explain the slow mutation rate of highly abundant proteins, weak protein (quinary) interactions are emergent properties of living cells. The protein complexes that result from quinary interactions are transient and thus difficult to study biochemically in vitro. Cross-correlated relaxation induced polarization transfer (CRIPT) based in-cell NMR allows the characterization of protein quinary interactions with atomic resolution inside live prokaryotic and eukaryotic cells. We showed that RNAs are an important component of protein quinary interactions. Protein quinary interactions are unique to the target protein and affect physicochemical properties, protein activity, and interactions with drugs.

Biography :

Email: ashekhtman@albany.edu