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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Journal Article
Solvent Electronic Polarization Effects on Na+–Na+ and Cl––Cl– Pair Associations in Aqueous Solution B
TL;DR: In this article, the formation of like-ion pairs in aqueous solution was studied by high-level ab initio methods, including classical molecular dynamics (MD), TIP5P, and QM/EFP MD (quantum mechanics/effective fragment potential molecular dynamics).
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Erratum: New Analytic Approximation to the Standard Molecular Volume Definition and Its Application to Generalized Born Calculations (Journal of Computational Chemistry (2003) 24:11 (1348-1356))
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The Unorthodox SNAP50 Zinc Finger Domain Contributes to Cooperative Promoter Recognition by Human SNAPC
Gauri W. Jawdekar,Andrej Hanzlowsky,Stacy Hovde,Blanka Jelencic,Michael Feig,James H. Geiger,R. William Henry +6 more
TL;DR: The results suggest that these eight cysteine and histidine residues perform different functions during DNA binding with those residues involved in zinc coordination likely performing a dominant role in domain stabilization and the others involved in DNA binding.
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Interactions of Amino Acid Side Chain Analogs within Membrane Environments
Vahid Mirjalili,Michael Feig +1 more
TL;DR: The interactions among four amino acid analog pairs within the membrane environment were investigated using umbrella sampling molecular dynamics simulations and generally expected qualitative trends of preferential association of polar compounds inside the membrane vs preferential interaction of hydrophobic compounds outside the membrane are confirmed.
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Role of conformational sampling of Ser16 and Thr17-phosphorylated phospholamban in interactions with SERCA.
Maryam Sayadi,Michael Feig +1 more
TL;DR: The results suggest that conformational changes in the cytoplasmic domain of PLB upon phosphorylation at Ser16 increase the likelihood of unfavorable interactions with SERCA in the E2 state prompting a conformational switch of SERCA from E2 to E1.