Daniel L. Parton
Memorial Sloan Kettering Cancer Center
14 Papers
13 Citations
Daniel L. Parton is an academic researcher from Memorial Sloan Kettering Cancer Center. The author has contributed to research in topics: Lipid bilayer & Biological membrane. The author has an hindex of 10, co-authored 14 publications. Previous affiliations of Daniel L. Parton include GlaxoSmithKline & University of Chicago.
Chat about Author
Papers
Aggregation of Model Membrane Proteins, Modulated by Hydrophobic Mismatch, Membrane Curvature, and Protein Class
TL;DR: Overall, it is clear that the nature and extent of membrane protein aggregation is dependent on several aspects of the proteins and lipids, including hydrophobic mismatch, protein class and shape, and membrane curvature.
141
Coarse-Grained Simulations of the Membrane-Active Antimicrobial Peptide Maculatin 1.1 ☆
TL;DR: Maculatin 1.1 is a membrane-active antimicrobial peptide from an Australian tree frog that forms a kinked amphipathic alpha-helix in the presence of a lipid bilayer or bilayer-mimetic environment, and to help elucidate its mechanism of membrane-lytic activity, a total of approximately 8 micros of coarse-grained molecular dynamics simulations of M1.1 were performed.
75
Formation of raft-like assemblies within clusters of influenza hemagglutinin observed by MD simulations.
TL;DR: It is suggested that a local aggregation of HA can be sufficient to drive association of the protein with raft-type lipids within the area of membrane spanned by the protein cluster, which may represent a general mechanism for the targeting of TM proteins to rafts in the plasma membrane, which is of functional importance in a wide range of cellular processes.
Multiscale simulations of the antimicrobial peptide maculatin 1.1: water permeation through disordered aggregates.
TL;DR: It is shown that water is able to permeate through the M1.1 aggregates by back-converting the CG configurations to atomistic representations, and investigation of aggregate stoichiometry shows that at least six peptides are required for water permeation.
Ensembler: Enabling High-Throughput Molecular Simulations at the Superfamily Scale.
TL;DR: The power of Ensembler is demonstrated by constructing models for all catalytic domains in the human tyrosine kinase family, using all available kinase catalytic domain structures from any organism as structural templates.