Dr. Scott comes to Saint Francis from Montana State University in Bozeman, MT where he researched the photophysical properties of fluorescent proteins as a postdoctoral fellow. He conducted extensive undergraduate research in physics at Louisiana Tech University in areas as diverse as
gravity wave physics, seismic analysis, solid state/materials physics, and high energy particle physics. Dr. Scott's graduate research at the University of Pennsylvania focused on experimental and theoretical investigations of the structure of water in biologically
important contexts, as well as the nature of the hydrogen bond itself. As a graduate student he also worked as a teaching assistant in graduate level chemistry and biochemistry classes.
Dr. Scott has published in a number of peer-reviewed chemistry journals, and he has presented at seminars and conferences in Pennsylvania, California, Montana, Alabama, Louisiana, Massachusetts, and Belgium. He is a member of the Biophysical Society, the American
Chemical Society, and the American Physical Society.
Scott, J.N.; Callis, P.R. MD+QM Investigations of the Length
Scale and Forcefield Dependence of the Time Dependent Fluorescent Stokes
Shift of Wild Type Staphylococcal Nuclease and Charge Mutants. Biophysical Journal (2015), 108(2) 622a.
Muiño, P.L.; Scott, J.N.; Callis, P.R. Fine-Grained
Spatial and Temporal Resolution of Water and Protein Contributions to
Ultra-Fast and Slower Fluorescence Shifts from MD + QM Simulations. Biophysical Journal 2014, 106(2) 205a.
Scott, J.N.; Callis, P.R. Insensitivity of Tryptophan Fluorescence to Local Charge Mutations. Journal of Physical Chemistry B 2013, 117 (33), 9598-605.
Scott, J.N.; Callis, P.R. MD+QM Calculations Explore the Origins of Differences Amongst the Red Fluorescent Proteins. Biophysical Journal (2013), 104(2) 684a.
Drobizhev, M.; Scott, J.N.; Callis, P.R.; Rebane, A. All-Optical Sensing of the Components of the Internal Local Electric Field in Proteins. IEEE Photonics Journal (2012), 4(5), 1996-2001.
Drobizhev, M.; Hughes, T.E.; Stepanenko, Y.; Wnuk, P.; O'Donell, K.;
Scott, J.N.; Callis, P.R.; Mikhaylov, A.; Dokken, L.; Rebane, A. Primary Role of the Chromophore Bond Length Alternation in Reversible Photoconversion of Red Fluorescence Proteins Nature Scientific Reports (2012), 2(688).
Drobizhev, M.; Hughes, T.E.; Rebane, A.; Davis, B.; Topol, I.; Scott, J.N.; Callis, P.R. Unified
Description Of Optical Properties and Photostability Of Fluorescent
Proteins By Means Of The Chromophore-Protein Electrostatic Interactions. Biophysical Journal (2012), 102(3) 403-4a.
Scott, J.N.; Callis, P.R. MD Simulations Reveal Ultrafast
Dielectric Compensation By Water Of Large Stokes Shifts From Charged
Groups In Staphylococcal Nuclease. Biophysical Journal (2012), 102(3) 734a.
Scott, J. Nathan; Vanderkooi, Jane M. Evidence of a Structural Defect in Ice VII and the Side Chain Dependent Response of Small Model Peptides to Increased Pressure. Applied Spectroscopy (2011), 65(7), 756-64.
Scott, J. Nathan; Vanderkooi, Jane M. A New Hydrogen Bond Angle/Distance Potential Energy Surface of the Quantum Water Dimer. WATER: A Multidisciplinary Online Journal (2010), Volume 2.
Vorobyev, Dmitriy Yu.; Kuo, Chun-Hung; Kuroda, Daniel G.; Scott, J. Nathan; Vanderkooi, Jane M.; Hochstrasser, Robin M. Water Induced Relaxation of a Degenerate Vibration ofGuanidinium Using 2D IR Echo Sectroscopy. Journal of Physical Chemistry B (2010), 114(8), 2944-53.
Vorobyev, Dmitriy Yu.; Kuo, Chun-Hung; Chen, Jian-Xin; Kuroda,
Daniel G.; Scott, J. Nathan; Vanderkooi, Jane M.; Hochstrasser, Robin M.
Ultrafast Vibrational Spectroscopy of a Degenerate Mode of Guanidinium Chloride. Journal of Physical Chemistry B (2009), 113(46), 15382-91.
Scott, J. Nathan; Nucci, Nathaniel V.; Vanderkooi, Jane M. Changes in Water Structure Induced by the Guanidinium Cation and Implications for Protein Denaturation. Journal of Physical Chemistry A (2008), 112(43), 10939-48.
Nucci, Nathaniel V.; Scott, J. Nathan; Vanderkooi, Jane M. Coupling
of Complex Aromatic Ring Vibrations to Solvent Through Hydrogen Bonds:
Effect of Varied On-Ring and Off-Ring Hydrogen-Bonding Substitutions. Journal of Physical Chemistry B (2008), 112(13), 4022-4035.
Dr. Scott's research interests are as varied as his background is diverse. He is currently investigating the optical properties of a class of proteins known as red fluorescent proteins. These proteins are ubiquitous in modern biochemistry, used world wide for a huge variety of
purposes, but the physical and dynamic properties that differentiate them are very poorly understood. Dr. Scott employs modern dynamic simulation techniques and quantum chemical methods to elucidate the optical and physical properties of these proteins using the
NSF-sponsored XSEDE system of computational resources, primarily the Gordon and Comet supercomputers at the San Diego Supercomputing Center.
Dr. Scott also maintains an interest in water structure, particularly water structure in unusual or extreme contexts, such as at extremely high pressures or temperatures. His interest in this area is motivated by the goal of understanding the physical limits to life as we know it
with respect to intensive quantities such as pressure and temperature. Dr. Scott has used a Diamond Anvil Cell (DAC) to investigate condensed phase systems at pressures of over 70,000 atmospheres and biological systems across a wide range of temperatures and pressures using
spectroscopic techniques. He is also interested in biomolecular structure and dynamics, and is currently using solution FTIR to study the side chain dependence of backbone dynamics in small model dipeptides while varying temperature, solvent viscosity, and confinement through
the use of reverse micelles.
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