S
Senthil K. Kandasamy
Researcher at University of Michigan
Publications - 21
Citations - 2753
Senthil K. Kandasamy is an academic researcher from University of Michigan. The author has contributed to research in topics: Lipid bilayer & Chemistry. The author has an hindex of 10, co-authored 11 publications receiving 2402 citations.
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Journal ArticleDOI
The MARTINI Coarse-Grained Force Field: Extension to Proteins
Luca Monticelli,Senthil K. Kandasamy,Xavier Periole,Ronald G. Larson,D. Peter Tieleman,Siewert-Jan Marrink +5 more
TL;DR: A new CG model for proteins as an extension of the MARTINI force field is developed and effectively reproduces peptide-lipid interactions and the partitioning of amino acids and peptides in lipid bilayers.
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Molecular dynamics simulations of model trans-membrane peptides in lipid bilayers : A systematic investigation of hydrophobic mismatch
TL;DR: Simulations of trans-membrane KALP peptides in phospholipid bilayers investigate hydrophobic mismatch alleviation mechanisms and reveal slower dynamics of both the peptide and lipid relative to those at a lower peptide/lipid ratio.
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Effect of salt on the interactions of antimicrobial peptides with zwitterionic lipid bilayers.
TL;DR: The studies indicate that while 50 ns simulations give information on peptide hydrogen bonding and lipid tail ordering that is insensitive to the initial peptide orientation, this run time is not sufficient to equilibrate the peptide position and orientation within the bilayer.
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Structure, topology, and tilt of cell-signaling peptides containing nuclear localization sequences in membrane bilayers determined by solid-state NMR and molecular dynamics simulation studies.
Ayyalusamy Ramamoorthy,Senthil K. Kandasamy,Dong Kuk Lee,Srikanth S. Kidambi,Ronald G. Larson +4 more
TL;DR: Results and simulations on the hydrophobic fragment of SA or SKP suggest that the tilt of helices increases with a decrease in bilayer thickness without changing the phase, order, and structure of the lipid bilayers.
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Binding and insertion of α-helical anti-microbial peptides in POPC bilayers studied by molecular dynamics simulations
TL;DR: The hydrogen bonding interactions between the lysines of the peptides and the oxygens of the polar lipid head-groups are the strongest and determine the overall peptide binding characteristics to the lipids.