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Richard M. Epand
Researcher at McMaster University
Publications - 521
Citations - 26937
Richard M. Epand is an academic researcher from McMaster University. The author has contributed to research in topics: Membrane & Peptide. The author has an hindex of 80, co-authored 515 publications receiving 25125 citations. Previous affiliations of Richard M. Epand include Brigham Young University & University of Edinburgh.
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Dependence of the bilayer to hexagonal phase transition on amphiphile chain length.
TL;DR: It is suggested that this is caused by a balance between increasing hydrocarbon volume promoting the HII phase through decreased intrinsic radius of curvature and greater relief of hydrocarbon packing constraints vs greater intermolecular interactions favoring the more condensed L alpha phase.
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Phospholipid structure determines the effects of peptides on membranes. Differential scanning calorimetry studies with pentagastrin-related peptides.
TL;DR: Perturbation of the thermotropic phase transition is strongest for dimyristoylphosphatidylglycerol, followed by the dipalmitoyl and the distearoyl analogs, and it is further reduced for dimmolecular hydrogen bonding.
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A comparison of the interaction of glucagon, human parathyroid hormone-(1-34)-peptide and calcitonin with dimyristoylphosphatidylglycerol and with dimyristoylphosphatidylcholine.
TL;DR: The results demonstrate that certain peptides can affect the phase transition properties of lipids in a manner similar to divalent cations, and overall hydrophobicity is not an overwhelming factor in determining the ability of peptides to interact with phospholipids.
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Induction of raft-like domains by a myristoylated NAP-22 peptide and its Tyr mutant.
TL;DR: The observation that formation of a PtdIns(4,5)P2‐rich domain is cholesterol dependent is extended and shows that it also leads to the formation of an cholesterol‐depleted domain, having important implications for the mechanism by which NAP‐22 affects actin reorganization in neurons.
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Absence of chiral domains in mixtures of dipalmitoylphosphatidylcholine molecules of opposite chirality
TL;DR: In this paper, the authors present calorimetric data for liposome mixtures of l-dipalmitoylphosphatidylcholine with perdeuterated hydrocarbon chains (l-DPPC-${\mathrm{d}}_{62}$) at varying molar concentrations and excess water (\ensuremath{\geqslant}30% by wt.