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faculty profile |
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| Dr. Andriy Baumketner |
| Assistant Professor |
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Department: Department of Physics and Opitical Science |
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Office: Grigg Hall 106 |
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Office Hours: |
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Email: abaumket@uncc.edu |
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Phone: 704-687-8294 |
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Personal Homepage |
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Research Description:
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) modeling of confinement effects on folding thermodynamics and kinetics
d) interactions of proteins with surfaces
f) theoretical models of folding kinetics
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Recent Publications:
J.-E. Shea, M. Friedel, A. Baumketner (2006). Simulations of protein folding. Rev. Comp. Chem. 22:169.
D.B. Teplow, N.D. Lazo, G. Bitan, S. Bernstein, T. Wyttenbach, M. T. Bowers, A. Baumketner, J.-E. Shea, B. Urbanc, L. Cruz, J. Borreguero, H.E. Stanley (2006). Elucidating amyloid beta-protein folding and assembly: A multidisciplinary approach. Acc. Chem. Res., 39:635.
A. Baumketner, J.-E. Shea (2006). Folding landscapes of the Alzheimer amyloid-beta(12-28) peptide. J. Mol. Biol., 362:567.
M. Friedel, A. Baumketner, J.-E. Shea (2006). Effects of surface tethering on protein folding mechanisms. PNAS, 103:839.
A. Baumketner, S.L. Bernstein, T. Wyttenbach, N.D. Lazo, D.B. Teplow, M.T. Bowers, J.-E. Shea (2006). Structure of the 21-30 fragment of amyloid Beta protein. Protein Science, 15:1239.
P. Soto, A. Baumketner, J.-E. Shea (2006). Aggregation of polyalanine in a hydrophobic environment. J. Chem. Phys., 124:134904.
A. Baumketner, S.L. Bernstein, T. Wyttenbach, G. Bitan, D.B. Teplow, M.T. Bowers, J.-E. Shea (2006). The structure of the wild type Amyloid-Beta monomer: a computational and experimental study. Protein Science, 15:420.
A. Baumketner, J.-E. Shea (2006). The thermodynamics of folding of a beta hairpin peptide probed through replica exchange molecular dynamics simulations. Theor. Chem. Acc. 116:262.
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Research Areas:
Amyloid
Computer Modeling
Protein Aggregation
Protein Folding
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