Richard N. Zare

Character introduction

Experience of education
Ph.D. Chemical Physics, Harvard University, 1963
B.A Chemistry and Physics, Harvard University, 1961
Positions
Marguerite Blake Wilbur Professor of Natural Science, Department of Chemistry and Department of Physics, Stanford University, Stanford, California
Adjunct Fellow, JILA, University of Colorado, Boulder, Colorado
Honors and Awards
2017  Othmer Gold Medal, Chemical Heritage Foundation
2016  Honorary Doctorate, University of Edinburgh, Edinburgh, Scotland
2013  Honorary Doctorate, University of South Florida, Tampa, Florida
2012  The International Science and Technology Cooperation Award of the People's Republic of China
2012   The World Academy of Sciences Lecture Medal
2012   The Torbern Bergman Medal, The Swedish Chemical Society, The Analytical Division
2011   King Faisal International Prize in Science
2010   R. B. Bernstein Award in Stereodynamics
2010   BBVA Foundation Frontiers of Knowledge Award in the Basic Sciences category
2010   Priestley Medal, American Chemical Society
2010  Theodore William Richards Medal, Northeastern Section of the American Chemical Society
2009   Presidential Award for Excellence in Science, Mathematics, and Engineering Mentoring (PAESMEM), U.S. Office of Science and Technology Policy
2009  F. A. Cotton Medal for Excellence in Chemical Research, Texas A&M University, Department of Chemistry, and Texas A&M Section, American Chemical Society
2008    George C. Pimentel Award in Chemical Education, American Chemical Society
2007    H. Julian Allen Award, NASA Ames Research Center
2007   Dudley R. Herschbach Award for Excellence in Research in the field of Collision Dynamics, Dynamics of Molecular Collisions Meeting, Santa Fe, New Mexico
2005   Chandler Medal, Department of Chemistry, Columbia University, New York, New York
2005   Pupin Medal, Columbia University School of Engineering, New York, New York
2005   Wolf Prize in Chemistry, Israel

Topic: Ultrafast Enzymatic Digestion Using Microdroplets

Abstract  The structural analysis of proteins is often accomplished by enzymatic digestion, but this procedure can take much time, and does not always give high sequence coverage. An example is the tryptic digestion of myoglobin, a protein containing 153 amino acid residues and a heme group with iron at its center.  Trypsin is known to cleave proteins after lysine and arginine amino acids measured from the C-terminus of the protein, provided that arginine or lysine is not followed by proline.  When an aqueous solution containing 10-µM myoglobin and 5-µg/mL trypsin is heated for 14 hours at 37°C, the sequence coverage is found to be only 60%.
I will describe an alternative approach developed by my research group in the Department of Chemistry, Fudan University, which relies on the use of aqueous microdroplets.  It is known that many reactions can be vastly accelerated in water microdroplets compared to the same reactions in bulk water. The reasons for this are many, but they are related to the unique environment of the air-water interface.  We find when the same solution containing trypsin and myoglobin is electrosprayed (-3 kV) at room temperature as tiny water microdroplets, we obtain 100% coverage in less than 1 ms, corresponding to a travel distance of 2 cm from the spray source to the inlet of the mass spectrometer. Other examples of ultrafast enzymatic digestion in microdroplets will be presented.


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