Janet Anderson

Janet S. Anderson

Job Title
Florence B. Sherwood Professor of Physical Sciences
Wold 221
Department/Program: Chemistry

Research interests

In collaboration with Griselda Hernãndez and David LeMaster at the Wadsworth Center, New York State Department of Health, Albany, NY, my students and I use molecular dynamics calculations, quantum calculations, and NMR data to investigate the structure and dynamics of proteins. I am interested in using Mathematica in Physical Chemistry courses, and in the integration of molecular modeling into all areas of the chemistry curriculum.

Courses:

CHM  60 Meals to Molecules
CHM 101 Introductory Chemistry I
CHM 102 Introductory Chemistry II
CHM 110H Accelerated Introductory Chemistry
CHM 351 Kinetics and Thermodynamics
CHM 352 Quantum Chemistry
CHM 354 Chemical Applications of Group Theory

    Recent Publications

    • Hernández, Griselda; Anderson, Janet S.; LeMaster, David M. (2009) “Polarization and Polarizability Assessed by Protein Amide Acidity”, Biochemistry48, 6482-6494.
    • LeMaster, David M.; Anderson, Janet S.; Hernández, Griselda (2009) “Peptide Conformer Acidity Analysis of Protein Flexibility Monitored by Hydrogen Exchange”, Biochemistry48, 9256-9265.
    • Janet S. Anderson, Griselda Hernández, and David M. LeMaster, “Structural model dependence of protein peptide acidity predictions for surface-exposed amides”, poster presented at the Proteins Gordon Research Conference, Holderness School, NH, June, 2009
    • Anderson, Janet S.; Hernández, Griselda; LeMaster, David M. (2010) Conformational Electrostatics in the Stabilization of the Peptide Anion, Current Organic Chemistry 14, 162-180.
    • Anderson, Janet S.; Hernández, Griselda; LeMaster, David M. (2010) Sidechain conformational dependence of hydrogen exchange in model peptides, Biophysical Chemistry151, 61-70.
    • Hernández, Griselda; Anderson, Janet S.; LeMaster, David M. (2010) Assessing the native state conformational distribution of ubiquitin by peptide acidity, Biophysical Chemistry 153, 70-82.
    • Janet S. Anderson, Griselda Hernández, and David M. LeMaster, “Sidechain conformational dependence of hydrogen exchange in model peptides”, poster presented at the 12th Annual Upstate NY NMR Symposium, SUNY Albany, Albany, NY, November 29, 2010.
    • Hernández, G., Anderson, J.S., and LeMaster, D.M. Electrostatics of Hydrogen Exchange for Analyzing Protein Flexibility. Invited chapter in Methods in Molecular Biology, 2011, Ed. Shektman, A. and Burz, D.S. (Humana Press).
    • Janet S. Anderson, Griselda Hernández, and David M. LeMaster, “Cumulative Probability Distribution Analysis of Model Protein Ensembles as Assessed by Peptide Acidity”, poster presented at the Gordon Research Conference—Computational Aspects of Biomolecular NMR”, Il Ciocco, Italy, May, 2011.
    • Hernández, Griselda; Anderson, Janet S.; LeMaster, David M. (2012) Experimentally assessing molecular dynamics sampling of the protein native state conformation, Biophysical Chemistry 163-164, 21-34.
    • Anderson, Janet S.; LeMaster, David M. (2012) Rotational Velocity Rescaling of Molecular Dynamics Trajectories for Direct Prediction of Protein NMR Relaxation, Biophysical Chemistry 168-169, 28-39.
    • Anderson, Janet S.; Hernández, Griselda; LeMaster, David M. (2013) Assessing the chemical accuracy of protein structures via peptide acidity, Biophysical Chemistry 171, 63-75.
    • Anderson, Janet S.; Mustafi, Sourajit M.; Hernández, Griselda; LeMaster, David M. (2014) Statistical allosteric coupling to the active site indole ring flip equilibria in the FK506-binding domain, Biophysical Chemistry 192, 41-48.

    Links

    • The Protein Data Bank(PDB) is a repository for all solved protein structures. It gives coordinates for all atoms and other information about the protein structure.
    • Mathematica is a program which can do both symbolic and numerical mathematics, with extensive graphics capabilities.
    • Spartan uses quantum mechanical and semi-empirical methods to model small molecules.

    Academic Credentials

    Ph.D., University of Wisconsin-Madison; B.S., College of William and Mary; Postdoctoral Research. Protein Computational Chemistry, Cornell University, 1976-1978