Michael Feig
Assistant Professor
- M.S. 1994, Technical University of Berlin
- Ph.D 1999, University of Houston
- Postdoctoral Fellow, 1999-2003, The Scripps Research Institute
- Alfred P.Sloan Fellow, 2005
feig@msu.edu
218 Biochemistry Building
Michigan State University
East Lansing, MI 48824-1319
Office: 517-432-7439
Lab: 517-353-6743
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Michael Feig
Research Interests
We are using computational methods in order to study the structure,
dynamics, and energetics of biological macromolecules such as proteins
or nucleic acids. Our focus is concentrated in two areas: 1) The modeling
of large supramolecular assemblies in atomic detail and 2) the accurate
prediction of native protein structures.
As
an example of a supramolecular complex we are investigating the interaction
between the E.coli mismatch recognition protein MutS and DNA
with mismatched or missing base pairs. MutS recognizes defective DNA
after replication and initiates a multi-step process that leads to DNA
repair. A detailed understanding of the DNA mismatch repair system is
relevant for some types of cancer where the repair process is compromised.
Starting from crystal structures of the MutS protein-DNA complex we
apply computer simulation techniques to look at energetic and dynamic
aspects of this system.
The prediction of protein structures from sequence has seen great progress
through
recent methodological advances and the availability of an increasing
number of structural templates from experimental protein structures.
It is now often possible to generate approximate predictions that capture
many of the general features of the native fold. MORE
Recent Publications
Zhou YC, Feig M, Wei GW. Highly accurate biomolecular electrostatics in continuum dielectric environments. J Comput Chem. (2008) Jan 15;291:87-97.
Tanizaki S, Clifford JW, Connelly BD, Feig M. Conformational Sampling of Peptides in Cellular Environments. Biophys J. (2008) Feb 1;94 3:747-59.
Olson MA, Feig M, Brooks CL 3rd. Prediction of protein loop conformations using multiscale modeling methods with physical energy scoring functions. J Comput Chem. 2007 Sep 17; [Epub ahead of print]
Stumpff-Kane AW, Maksimiak K, Lee MS, Feig M. Sampling of near-native protein conformations during protein structure refinement using a coarse-grained model, normal modes, and molecular dynamics simulations. Proteins. 2007 Sep 17;70(4):1345-1356.
Wittayanarakul K, Hannongbua S, Feig M. Accurate prediction of protonation state as a prerequisite for reliable MM-PB(GB)SA binding free energy calculations of HIV-1 protease inhibitors. J Comput Chem. 2007 Sep 11; [Epub ahead of print]
Michael Feig: Kinetics from Implicit Solvent Simulations of Biomolecules as a Function of Viscosity Journal of Chemical Theory and Computation (2007) 3, 1734-1748.
Montero-Moran GM, Li M, Rendon-Huerta E, Jourdan F, Lowe DJ, Stumpff-Kane AW, Feig M, Scazzocchio C, Hausinger RP. Purification and Characterization of the Fe(II)- and alpha-Ketoglutarate-Dependent Xanthine Hydroxylase from Aspergillus nidulans. Biochemistry. (2007) 8;46(18):5293-5304.
Chocholousova J, Feig M. Implicit solvent simulations of DNA and DNA-protein complexes: agreement with explicit solvent vs experiment. J Phys Chem B. (2006) 110(34):17240-51.
Jawdekar GW, Hanzlowsky A, Hovde SL, Jelencic B, Feig M, Geiger JH, Henry RW. The unorthodox SNAP50 zinc finger domain contributes to cooperative promoter recognition by human SNAPC. J Biol Chem. (2006) 281(41):31050-60.
Muller TA, Zavodszky MI, Feig M, Kuhn LA, Hausinger RP. Structural basis for the enantiospecificities of R- and S-specific phenoxypropionate/alpha-ketoglutarate dioxygenases. Protein Sci. (2006) 15(6):1356-68.
Jankun J, Aleem AM, Malgorzewicz S, Szkudlarek M, Zavodszky MI, Dewitt DL, Feig M, Selman SH, Skrzypczak-Jankun E. Synthetic curcuminoids modulate the arachidonic acid metabolism of human platelet 12-lipoxygenase and reduce sprout formation of human endothelial cells. Mol Cancer Ther. (2006) 5(5):1371-82. MORE