Josh Wand was born and raised in Ottawa, Canada. He received his B.Sc. (Hons) in biochemistry from Carleton University in Ottawa.
Working under the direction of Stan Tsai, he also received a M.Sc. in bioorganic chemistry from Carleton University. He received his Ph.D. in biophysics from the University of Pennsylvania under the guidance of Walter Englander.
After a short postdoctoral stint in solid state NMR at the National Research Council of Canada with I.C.P. Smith, he joined the faculty of the Institute for Cancer Research. He subsequently spent time on the faculties of the University of Illinois at Urbana-Champaign and the State University of New York at Buffalo.
He is currently the Benjamin Rush Professor of Biochemistry & Biophysics where he continues to employ novel applications of solution NMR to questions in protein biophysics.
Welcome to the Wand Lab. Our research group focuses on novel applications of high resolution solution and solid state NMR techniques to fundamental problems in biophysics. Our interest in protein biophysics include the on-going development of reverse micelle encapsulation to study the structure & dynamics of large soluble proteins, integral and anchored membrane proteins and their complexes; the use of advanced NMR relaxation techniques to characterize the internal dynamics of proteins and employ the "dynamical proxy" as an "entropy meter" to explore the role of conformational entropy in the energetics of protein-ligand interactions; to develop and use hydrogen-exchange based methods to journey over the protein energy landscape in a variety of contexts; to understand the role of solvent in maintaining the structural and dynamic integrity of proteins; applications of protein design and engineering in a variety of contexts.
We are also active in the development of sensitivity optimized sparse NMR data acquisition, high pressure NMR apparatus and applications and computer-assisted NMR data analysis.
| Office Suite | |
| 905 Stellar-Chance Labs Department of Biochemistry & Biophysics University of Pennsylvania School of Medicine 422 Curie Blvd. Philadelphia, PA 19104-6059 F: 215-573-7290 |
Professor Josh Wand wand@mail.med.upenn.edu T: 215-573-7288 |
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| Molecular Biology Lab | |
| 904 Stellar-Chance Labs Department of Biochemistry & Biophysics University of Pennsylvania School of Medicine 422 Curie Blvd. Philadelphia, PA 19104-6059 T: 215-573-7289 |
Dr. Sabrina Bedard sabrina.bedard@gmail.com |
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| NMR Lab | |
| G6 Blockley Hall Department of Biochemistry & Biophysics University of Pennsylvania School of Medicine 423 Curie Blvd. Philadelphia, PA 19104-6059 T: 215-573-5969 |
Dr. Kathy Valentine valen@mail.med.upenn.edu T: 215-573-5971 |
Highlight paper
Nathaniel V. Nucci, Maxim S. Pometun, and A. Joshua Wand (2011) Site-resolved measurement of water-protein interactions by solution NMR. Nat. Struct. Mol. Biol. 18:245-249
The interactions of biological macromolecules with water are fundamental to their structure, dynamics and function. Historically, characterization of the location and residence times of hydration waters of proteins in solution has been quite difficult. Solution NMR has long held promise but has been severely plagued by seemingly insurmountable problems. Confinement within the nanoscale interior of a reverse micelle slows water dynamics, allowing detection of global protein-water interactions using nuclear magnetic resonance techniques. Complications that normally arise from hydrogen exchange and long-range dipolar coupling are overcome by the nature of the reverse micelle medium.
Characterization of the hydration of ubiquitin demonstrates that encapsulation within a reverse micelle allows detection of dozens of hydration waters. Comparison of nuclear Overhauser effects obtained in the laboratory and rotating frames indicate a considerable range of hydration water dynamics is present on the protein surface. In addition, an unprecedented clustering of different hydration dynamic classes of sites is evident.