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Rainer A. Böckmann

Researcher at University of Erlangen-Nuremberg

Publications -  80
Citations -  5904

Rainer A. Böckmann is an academic researcher from University of Erlangen-Nuremberg. The author has contributed to research in topics: Lipid bilayer & Membrane. The author has an hindex of 30, co-authored 74 publications receiving 4916 citations. Previous affiliations of Rainer A. Böckmann include Max Planck Society & Saarland University.

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Low free energy barrier for ion permeation through double-helical gramicidin.

TL;DR: The energetics of single potassium ion permeation by means of the potential of mean force (PMF) for both gramicidin conformations embedded in a DMPC bilayer has been addressed by molecular dynamics simulations and a significantly decreased free energy barrier for potassium ion passage through DH as compared to HD is reported.
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Serotonin Alters the Phase Equilibrium of a Ternary Mixture of Phospholipids and Cholesterol.

TL;DR: The results demonstrate that small membrane binding molecules such as neurotransmitters have a profound impact on essential membrane properties and suggests a mechanism by which the interaction of small molecules with membranes can influence the function of membrane proteins and non-cognate receptors.
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Peptide-induced membrane curvature in edge-stabilized open bilayers: A theoretical and molecular dynamics study

TL;DR: It is proved that open-edged patches evolve from a planar state to a closed vesicle, with a transition rate that strongly depends on the concentration of lipid soluble peptides, for close-to-critical values for the patch size and edge energy.
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Evidence for proton shuffling in a thioredoxin-like protein during catalysis.

TL;DR: The results support the view of an internal proton shuffling mechanism during oxidation crucial for the uptake of two electrons from the substrate protein and suggest a functional role of hydration entropy of active-site groups.
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Exploring the Formation and the Structure of Synaptobrevin Oligomers in a Model Membrane.

TL;DR: Higher-order oligomeric models (ranging from pentamer to octamer), built by incremental addition of peptides to smaller oligomers, revealed substantial stability and high compactness, and larger sybII oligomers may induce membrane deformation, thereby possibly facilitating fast fusion exocytosis.