Biosketch
Arthur G. Palmer, Ph.D. is the Robert Wood Johnson, Jr. Professor of Biochemistry and Molecular Biophysics at Columbia University Irving Medical Center. He received a B. A. (Magna cum Laude) in Chemistry from Haverford College in 1980; an M. S. in Industrial Health from University of Michigan in 1986 and Ph.D. in Chemistry from University of North Carolina, Chapel Hill in 1989. Palmer was an NSF Postdoctoral Fellow with Dr. Peter E.. Wright in the Department of Molecular Biology of The Scripps Research Institute from 1989-1992. Palmer joined Columbia University as an Assistant Professor in 1992, was promoted to Associate Professor in 1998 and to Professor in 2002. He was appointed to the Robert Wood Johnson Jr. Chair in 2009. Palmer served as Acting Chair of Biochemistry and Molecular Biophysics from 2003-2009 and from 2018-2022. He served as Associate Dean for the Coordinated Doctoral Programs in Biomedical Sciences from 2012-2024 and has served as Director of NMR spectroscopy at the New York Structural Biology Center since 2010. Palmer has received the EAS Award for Outstanding Achievement in Magnetic Resonance, the Charles W. Bohmfalk Excellence in Teaching Award of Columbia University, the Gunther Laukien Prize, Experimental NMR Conference (ENC), the Nakanishi Prize of the American Chemical Society, and is an elected Fellow of the International Society of Magnetic Resonance (ISMAR). In addition to teaching at Columbia University, Palmer has taught in more than 30 short courses on biological NMR spectroscopy around the world.
Research Interests
Arthur G. Palmer uses NMR spectroscopy, molecular dynamics simulations, and biophysical techniques to elucidate the coupling between conformational dynamical properties and biological functions of proteins and other biological macromolecules. His research extends from development of novel methods in NMR spectroscopy; to computational and theoretical analyses of protein dynamics; and to applications to protein folding, molecular recognition, and enzymatic catalysis. He introduced modern robust statistical approaches for data analysis of NMR spin relaxation data and pioneered thermodynamic interpretations of spin relaxation to characterize intramolecular conformational entropy of macromolecules. Investigation of dynamic properties of proteins on biologically important microsecond-millisecond time scales has been revolutionized through the development by Palmer and coworkers of new experimental and theoretical approaches for the measurement and interpretation of chemical exchange phenomena. Palmer has a longstanding interest in the stability and activity of ribonuclease H enzymes from organisms adapted for life indifferent thermal environments and in dynamic contributions to molecular recognition by transcription factors, including the bZip and Hox protein families. His research contributions also include mechanisms of strand swapping in the cell-adhesion cadherin superfamily, mechanisms of substrate order-of-addition in the AlkB superfamily, and kinetics of protein folding.
Membership Type
Member
Election Year
2024
Primary Section
Section 29: Biophysics and Computational Biology