MED Researchers

Andriy Baumketner

Andriy Baumketner

704-687-8294
CBES Area of Expertise:

Atomistic simulations of protein folding; computational studies of protein aggregation; theoretical models of chaperon-assisted folding; interactions of proteins with surfaces and models of folding kinetics.

 

CBES Area of Interest:

The research interests of my group are in theoretical approaches to problems in biological and chemical physics. Our recent efforts have focused on a) atomistic simulations of protein folding, b) computational studies of protein aggregation, c) theoretical models of chaperon-assisted folding, d) interactions of proteins with surfaces and e) models of folding kinetics.


Wei Cai, Ph.D.

Wei Cai, Ph.D.

704-687-4581
CBES Area of Expertise:

Development of fast numerical methods for electrostatics interactions and hybrid salvation models for biomolecules.

CBES Area of Interest:

Biomedical applications that include multiscale modeling and computational biology.


Shaozhong Deng, Ph.D.

Shaozhong Deng, Ph.D.

704-687-6657
CBES Area of Expertise:

Computational structural biology, in particular, hybrid explicit/implicit solvent method for biomolecular simulations. 

CBES Area of Interest:

Working on computational structural biology, in particular, on hybrid explicit/implicit solvent methold for biomolecular simulations.


Donald J. Jacobs, Ph.D.

Donald J. Jacobs, Ph.D.

704-687-8143
CBES Area of Expertise:

Biophysical modeling involving development of algorithms for computational biology applications.

CBES Area of Interest:

My research centers on biophysical modeling involving development of algorithms for computational biology applications.  My main activity is funded by the National Institutes of Health to develop “FAST” software that provides a Flexibility and Stability Test for proteins with known three-dimensional structure to predict their thermodynamic and mechanical properties within a cellular environment.  Our FAST predictions reveal Quantitative Stability/Flexibility Relationships (QSFR).  A QSFR database augmented with bioinformatics and statistical analysis tools is being developed.  Through FAST/QSFR we can obtain improved descriptions of protein structure/function relationships, protein-substrate association and the protein folding/unfolding process. Our methods will facilitate novel homology modeling schemes, better sequence and structural alignment tools, and prediction of protein oligomerization states and their associated changes in stability and flexibility. Together, our FAST software and QSFR database will support myriad biologically significant applications in pharmacology and rational protein design including engineering of highly stable enzyme catalysts for industrial purposes.


Joanna Krueger, Ph.D.

Joanna Krueger, Ph.D.

704-687-4913
CBES Area of Expertise:

Biophysical Chemistry

CBES Area of Interest:

Structural information on biomolecular associations using the techniques of small-angle  X-ray and neutron scattering, chemical cross-linking with peptide analysis by MS, selected-site mutagenesis and spectroscopy (FTIR, CD, UV-VIS); and visualized through the use of molecular modeling.


Dennis Livesay, Ph.D.

Dennis Livesay, Ph.D.

704-687-7995
CBES Area of Expertise:

Protein functional site prediction algorithms; robust motif-based comparative bioinformatic strategies, and improved sequence alignment strategies.

CBES Area of Interest:

Much of our work is focused in these areas, specifically development of: (a) protein functional site prediction algorithms, (b) robust motif-based comparative bioinformatic strategies, and (c) improved sequence alignment strategies.


Yuri Nesmelov, Ph.D.

Yuri Nesmelov, Ph.D.

704-687-5886
CBES Area of Expertise:

Spectroscopy of electron paramagnetic resonance, optical spectroscopy, biophysics of molecular motors.

CBES Area of Interest:

My research interests are focused on biological molecular motors. I study myosin, the protein responsible for force generation in muscle, cell locomotion and intracellular trafficking. I combine protein mutagenesis, site directed labeling, multifrequency electron paramagnetic resonance (EPR) and transient time-resolved fluorescence resonance energy transfer (TR2FRET) to explore myosin functional dynamics on molecular and submolecular level. The ultimate goal of these studies is to determine the mechanism of force generation in myosin.  I am also interested in manipulating of microwave field distribution in EPR cavity to maximize sensitivity of EPR measurement for aqueous samples, through the sample geometry optimization and usage of ferroelectric/dielectric cavity inserts.