Monday, September 14 & Tuesday, September 15 with David Russell
The University of Utah's Department of Chemistry were pleased on September 14th and 15th to welcome David Russel from Texas A&M University to present at the J. Calvin Giddings Lectureship. The J. Calvin Giddings Lectureship was established in the year 2000 and ever since has hosted outstanding scientist speakers. Professor Russel shared his work on Dynamics of Protein-Ligand Interactions: Lessons from “Native” Mass Spectrometry and New Vista in Native Mass Spectrometry: Impact of Advanced Technologies.
Professor J. Calvin Giddings was a graduate of Brigham Young University, earned his Ph.D. under Henry Eyring at the University of Utah in 1954, and did postdoctoral work at the University of Wisconsin. He joined the faculty of the University of Utah in 1957. Among analytical chemists, Professor Giddings was best known as a pioneer in chromatography and separations, particularly in theory and teaching. Giddings established the journal Separation Science and Technology and was editor for over 30 years. He authored over 400 scientific publications, including the theoretical landmark books Dynamics of Chromatography, and Unified Separation Science, widely used in graduate-level separation courses. He also invented Field Flow Fractionation and led the way in its development and application.
David Russell
David Russell is a MDS Sciex Professor of Mass Spectrometry in the Departent of Chemistry, Texas A&M University. His research focuses on fundamentals of mass spectrometry, ion mobility-mass spectrometry, analytical and biophysical chemistry. He serves as Director of the Laboratory of Biological Mass Spectrometry and is a principal investigator for the NIH RM1 Center for Mass Spectrometry Guided Structural Biology. His current research emphasizes proteins and protein complexes, which includes development of advanced mass spectrometry methods and technologies for studies of the solution dynamics of proteins and large protein complex (KDa to MDa complexes).
Dynamics of Protein-Ligand Interactions: Lessons from “Native” Mass Spectrometry
Abstract: The research aims focus on development of integrated instrumentation for studies of protein/protein complex dynamics in solution. Lessons learned from Prof. J. Calvin Giddings during my Ph. D graduate studies motivated much of our current research, specifically roles of temperature, solvent (H2O/D2O) and co-solutes that alter the dynamics of proteins in solution, including hydrophobic interactions of alkyl ammonium ions with proteins and protein complexes... lessons taught by Prof. J. Calvin Giddings. These research aims motivated our development of variable-temperature-ESI, whereby temperature of the solution contained in the ESI emitter can be accurately varied between 2 – 98o C. Further motivation... how do solution conditions (H2O or D2O) and the presence of cosolutes (native ESI “buffers”) influence dynamics of protein/protein complex dynamics? For decades, we and others have sought answers to Fred McLafferty’s question (PNAS 2008) “...for how long, under what conditions and to what extend, can solution structure be retained without solvent”... caveat...we do not know the solution structure(s)...it’s not a question of structure, its more about dynamics...activated by interactions involving H2O “...the lubricant of life!” (G. Wilson 1997...and many variants on this theme!).
New Vista in Native Mass Spectrometry: Impact of Advanced Technologies
Abstract: The research aims focus on development of integrated instrumentation for studies of protein/protein complex dynamics in solution. Lessons learned from Prof. J. Calvin Giddings during my Ph. D graduate studies motivated much of our current research, specifically roles of temperature, solvent (H2O/D2O) and co-solutes that alter the dynamics of proteins in solution, including hydrophobic interactions of alkyl ammonium ions with proteins and protein complexes... lessons taught by Prof. J. Calvin Giddings. These research aims motivated our development of variable-temperature-ESI, whereby temperature of the solution contained in the ESI emitter can be accurately varied between 2 – 98o C. Further motivation... how do solution conditions (H2O or D2O) and the presence of cosolutes (native ESI “buffers”) influence dynamics of protein/protein complex dynamics? For decades, we and others have sought answers to Fred McLafferty’s question (PNAS 2008) “...for how long, under what conditions and to what extend, can solution structure be retained without solvent”... caveat...we do not know the solution structure(s)...it’s not a question of structure, its more about dynamics...activated by interactions involving H2O “...the lubricant of life!” (G. Wilson 1997...and many variants on this theme!).
Hosts: Gabe Nagy & Peter Armentrout
History of Giddings Lecture Speakers at the University of Utah
2026
Pat Unwin, University of Warwick
The Long and Winding Road to Nanoscale Electrochemistry and Tales of the Unexpected: The Continuing Story of Electrochemistry at Carbon Electrodes
2025
Evan Williams, University of California-Berkley
Overcoming Molecular Complexity One Ion at a Time and A Window into Molecular Complexity with Mass Spectrometry: From Physics to Chemistry to Biology and Beyond
2023-2024
Marc Koper, Leiden University
How to understand rates of electrocatalytic reactions & How to make green hydrogen
2022-2023
2020-2021
Structural Characterization of Lipids, Nucleic Acids, Proteins, and Molecular Machines using Ion/Ion Chemistry
2019-2020
Jeanne Pemberton, University of Arizona
Fun with Sugars: Some Mundane and Not-So-Mundane New Materials from Glycolipids
2017-2018
Nanostructured Mesoscale Optical Materials
Operando Methods for The Study of Energy Materials & The Energy Landscape in the Age of Sustainability
2014-2015
Surfaces: The work of the devil?
2013-2014
Chromatography: the transport processes that make it work & Submicrometer silica particles in protein electrophoresis
2011-2012
Chemical Cytometry - the Analysis of the Content of Single Cells & The Role of Analytical Chemistry in Sequencing the Human Genome
2010-2011
Electrochemical Surface-Enhanced Raman Spectroscopy: Past, Present and Future & Nanostructure-Enhanced Raman Spectroscopy: Towards a Versatile Analytical Strategy
2007-2008
Nanoplasmonics: From Physics to DNA Diagnostics
2005-2006
Making it Count: Quantitation of Low-Copy-Number Proteins in Single Cells
2000-2001
The inaugural speaker of the lecture
Analytical Glycobiology: a Methodological Frontier & Exploring the Limits of Separating Power: A Scientific Legacy of J. Calvin Giddings