Nicholas Levinson, PhD

Associate Professor, Department of Pharmacology

Nicholas Levinson

Contact Info

Office Phone 612-301-1322

Office Address:
3-118 Nils Hasselmo Hall
312 Church St SE
Minneapolis, MN 55455

Lab Address:
3-266 Nils Hasselmo Hall
312 Church St SE
Minneapolis, MN 55455

PhD, University of California, Berkeley


Dr. Levinson is an Associate Professor in the Department of Pharmacology and a member of the Masonic Cancer Center’s Genetic Mechanisms Program. Dr. Levinson received his Bachelors and Masters degrees in Biochemistry from Cambridge University, and his PhD degree from the University of California, Berkeley, where he studied the structural basis of protein kinase function. After postdoctoral training at Stanford University in the Department of Chemistry, he joined the University of Minnesota as an Assistant Professor in 2014. 


Protein kinase structural dynamics and allostery, kinase inhibitor targeting, protein crystallography, magnetic resonance, infrared spectroscopy and ultrafast fluorescence spectroscopy

Awards & Recognition

NIH R33 Grant CA246363, 2020

Medical School’s Faculty Research Development Grant, 2019

Dean’s first-R01 Award, UMN Medical School 130th Anniversary, 2018

NIH R01 Grant GM121515 2017

NIH R21 Grant CA217695 2017

NIH K99 Pathway to Independence Award, 2012-2017

NIH NRSA F32 Award, 2009-2011


Research Summary/Interests

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.