M
Michael Feig
Researcher at Michigan State University
Publications - 193
Citations - 28987
Michael Feig is an academic researcher from Michigan State University. The author has contributed to research in topics: Molecular dynamics & Solvation. The author has an hindex of 54, co-authored 181 publications receiving 24201 citations. Previous affiliations of Michael Feig include Scripps Research Institute & RIKEN Quantitative Biology Center.
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Book ChapterDOI
Implicit Solvent Simulations of Biomolecules in Cellular Environments
TL;DR: Implicit solvent models have become popular in molecular dynamics simulations and related applications as discussed by the authors, in particular, implicit solvent methods based on the Generalized Born formalism are increasingly employed in simulation of biological macromolecules in aqueous solvent.
Journal ArticleDOI
Conformational Sampling of Influenza Fusion Peptide in Membrane Bilayers as a Function of Termini and Protonation States
Afra Panahi,Michael Feig +1 more
TL;DR: It is found that the influenza fusion peptide mostly adopts helical structures with a pronounced kink at residues 11-13 with both N- and C-terminal helices oriented mostly parallel to the membrane surface.
Journal ArticleDOI
Molecular Dynamics Trajectory Compression with a Coarse-Grained Model
TL;DR: In this article, trajectory compression based on conversion to the coarse-grained model PRIMO is proposed, which largely preserves structural features and to a more limited extent also energetic features of the original trajectory.
Journal ArticleDOI
Substrate specificity of SpoIIGA, a signal-transducing aspartic protease in Bacilli.
TL;DR: By co-expressing proteins in Escherichia coli, it was shown that charge reversal substitutions for acidic residues 24 and 25 of Pro-σ(E), and for basic residues 245 and 284 of SpoIIGA, impaired cleavage, consistent with a model predicting possible electrostatic interactions between these residues.
Journal ArticleDOI
Crowding affects structural dynamics and contributes to membrane association of the NS3/4A complex
TL;DR: In this article, the authors describe how crowded environments affect the internal dynamics and diffusion of the hepatitis C virus proteases NS3/4A and suggest that crowding may assist in the formation of an NS4A helical fragment, positioned exactly where a transmembrane helix would fold upon contact with the membrane.