Current Position:

• Dean of the Graduate School (http://www.umt.edu/grad/)

• Director of the A.P.  Sloan Scholars Program for Native American graduate students in STEM disciplines at The University of Montana (http://www.umt.edu/grad/SIGP/default.php)

• Professor of Chemistry and Biochemistry, The University of Montana at Missoula (http://www.cas.umt.edu/chemistry/default.html)

• Director,  BioSpectroscopy Core Research Laboratory (http://cas.umt.edu/departments/cbsd/facilities/biospectroscopy/default.html)

Description:

J.B. Alexander (Sandy) Ross joined The University of Montana Department of Chemistry and Biochemistry in 2001 as Professor and Director of the BioSpectroscopy Core Laboratory and became Associate Dean of the Graduate School in 2010 and Dean in 2012. Previously, he was Professor of Biochemistry and Molecular Biology and Co-Director of the Biophysics, Structural Biology, and Biomathematics Training Program at Mount Sinai School of Medicine in New York.

Sandy earned his Ph.D. at the University of Washington in 1976 under the joint supervision of D.A. Deranleau and D.C. Teller. He carried out postdoctoral research under the direction of A.L. Kwiram at the University of Washington, L. Brand at The Johns Hopkins University, and P.H. Petra at the University of Washington. He has been a Visiting Professor at the University of Parma, Italy, and a Visiting Scientist at the National Synchrotron Light Source at Brookhaven National Laboratory.

Sandy is a physical biochemist specializing in time-resolved excited-state spectroscopy and single-molecule experiments. He is an investigator in the Center for Biomolecular Structure and Dynamics and the Center for Structural and Functional Neuroscience at The University of Montana.

Field Of Study:

Physical Biochemistry

Analytical Biochemistry

Biological Fluorescence

Biothermodynamics

Research Interests:

Our research concerns understanding how conformational dynamics and interactions of biological molecules regulate their function. Our approach is to use a combination of experimental and computational biophysical methods: we specialize in time-resolved and single-molecule fluorescence spectroscopies; we collaborate with others who specialize in X-ray crystallography, NMR, analytical ultracentrifugation, inorganic chemistry and computational chemistry.

Novel Probes for Studying Dynamics on the Submicrosecond-to-Microsecond Time Scales: Because fluorescence occurs in the ps to tens-of-ns time range, lifetime measurements can provide information about local (specific site) motions (ps to a few ns) and global motions of macromolecules with molecular weights up to 100 kDa (~50 ns). To study the dynamics of larger macromolecules and assemblies that occur in 100-ns to 10-ms time-range, in collaboration with the Rosenberg group at The University of Montana, we have been developing luminescent probes based on organo-metal complexes that have lifetimes spanning this longer time-range and that have high quantum yields and polarized emission. These novel probes are being used to study the dynamics of membrane proteins incorporated in nanodiscs, described below.

Membrane-Protein Interactions and dynamics: In collaboration with the Atkins group at the University of Washington, we are using time-resolved fluorescence microscopy and single-molecule fluorescence spectroscopy to study the conformational dynamics and interactions of recombinant receptors and transporters incorporated in nanodiscs. Nanodiscs, largely developed by Sligar and collaborators at the University of Illinois, are mono-disperse, aqueous-soluble assemblies of nm-scale, protein-belted, phospholipid bilayers. The belt proteins are recombinant constructs based on high-density apolipoprotein A1. The easily controlled lipid composition and stable properties of nanodiscs make them particularly useful for biophysical study of membrane proteins.Structural dynamics and enzyme catalysis: G proteins. Correlated motions ranging in time scales from picoseconds to microseconds have been shown to be critical in overcoming activation energy barriers to substrate binding and active site pre-organization for catalysis in enzymes with turnover rates in the microsecond to millisecond range. In a multi-investigator collaboration led by the Sprang group, our group is using single-molecule fluorescence spectroscopy to discern the fluctuations in the structure of the alpha subunit of the G protein, Ga, over the ps-s time scale, in substrate-bound and product-bound complexes and during nucleotide release, Our goal is to characterize these states with respect to their dynamics times and the protein domains, segments and residues involved.

 

 

 

Courses:

Bioc 581    Physical Biochemistry

Education:

B.A.: Antioch College, Yellow Springs

Ph.D.: University of Washington, Seattle

Post-Doctoral: University of Washington, Seattle; The Johns Hopkins University

Teaching Experience:

Biochemistry and physical biochemistry since 1982

Affiliations:

American Chemical Society

Biophysical Society

Sigma Xi
 

Professional Experience:

Visiting Scientist:

National Synchrotron Light Source, Brookhaven National Laboratory

University of Parma

University of Torino

Consulting:

Fluorescence Innovations - time-resolved fluorescence

Quantum Northwest - fluorescence instrumentation

Darby & Darby – intellectual property

Fluorescence Unlimited – time-resolved fluorescence in clinical chemistry

Executive Editor, Analytical Biochemistry

Associate Editor, Cell Biochemistry and Biophysics
 

 

Honors/Awards:

A.P. Sloan Mentor of the Year (Compact for Faculty Diversity Institute, 2010)

Selected Publications:

Manhat BA, Brown AL, Black LA, Ross JBA, Fichter K, Vu T, Richman E, Goforth AM: One-step Melt Synthesis of Water Soluble, Photoluminescent, Surface-Oxidized Silicon Nanoparticles for Cellular Imaging Applications. Chem Mater, 23:2407–2418, 2011.

Wang H, Lu M, Tang M-S, Van Houten B, Ross JBA, Le XC: DNA Wrapping on UvrB, Mediated by UvrA, is an Early Event in the Damage Recognition Pathway during E. coli Nucleotide Excision Repair. Proc Natl Acad Sci USA, 106:12849-12854, 2009.          

Sharmin A, Darlington RC, Hardcastle KI, Ravera M, Rosenberg E, Ross JBA: Tuning Photophysical Properties with Ancillary Ligands in Ru(II) Mono-Diimine Complexes. J Organometallic Chem, 694:988-1000, 2009.

Minazzo A, Darlington RC, Ross JBA: Loop Dynamics of the Extracellular Domain of Human Tissue Factor and Activation of Factor VIIa.  Biophysical J, 96:681-692, 2009.

Sharmin A, Minazzo A, Salassa L, Rosenberg E, Ross JBA, Shariff SE, Hardcastle KI: Synthesis, Structure, Photophysical and Electrochemical Behavior of 2-amino-Anthracene Triosmium Clusters. Inorg Chim Acta 361: 1624-1633, 2008.

Garino C, Gobetto R, Nervi C, Salassa L, Rosenberg E, Ross JBA, Chu X, Hardcastle KI, Sabatini C: Spectroscopic and Computational Studies of a Ru(II)Terpyridine Complex: The Importance of Weak Intermolecular Forces to Photophysical Properties. Inorg Chem 46:8752-8762, 2007.

Senear DF, Tretyachenko-Ladokhina V, Opel ML, Aeling KA, Hatfield GW, Franklin LM, Darlington RC, Ross JBA: Pressure Dissociation of Integration Host Factor-DNA Complexes Reveals Flexibility-Dependent Structural Variation at the Protein-DNA Interface. Nucleic Acids Research 35:1761-1772, 2007.

Gobetto R, Caputo G, Garino C, Ghiani S, Nervi C, Salassa L, Rosenberg E, Ross JBA, Viscardi G, Martra G, Miletto, Milanesio M: Synthesis, Electrochemical and Electrogenerated Chemi-luminescence Studies of Ruthenium(II) Bis(2,2’-bipyridyl){2-(4-methylpyridin-2-yl)benzo[d]-X-azole} Complexes. Eur J Inorg Chem, 2839-2849, 2006.

Garino C, Gobetto R, Nervi C, Salassa L, Croce G, Milanesio M, Rosenberg E, Ross JBA: Solid State Structure, Quantum Calculations and Spectroscopic Characterization of the Hydrogen Bonded [Os(bpy)2(CO)(EtO···H-DMAP)][PF6]2 Complex. Eur J Inorg Chem, 138:606-614, 2005.