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Gerhard Hummer

Researcher at Max Planck Society

Publications -  458
Citations -  40888

Gerhard Hummer is an academic researcher from Max Planck Society. The author has contributed to research in topics: Molecular dynamics & Medicine. The author has an hindex of 93, co-authored 416 publications receiving 34375 citations. Previous affiliations of Gerhard Hummer include National Institutes of Health & Center for Information Technology.

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Water conduction through the hydrophobic channel of a carbon nanotube

TL;DR: Observations suggest that carbon nanotubes, with their rigid nonpolar structures, might be exploited as unique molecular channels for water and protons, with the channel occupancy and conductivity tunable by changes in the local channel polarity and solvent conditions.
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Guidelines for the use and interpretation of assays for monitoring autophagy (4th edition)

Daniel J. Klionsky, +2983 more
- 08 Feb 2021 - 
TL;DR: In this article, the authors present a set of guidelines for investigators to select and interpret methods to examine autophagy and related processes, and for reviewers to provide realistic and reasonable critiques of reports that are focused on these processes.
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System-Size Dependence of Diffusion Coefficients and Viscosities from Molecular Dynamics Simulations with Periodic Boundary Conditions

TL;DR: In this paper, the system-size dependence of translational diffusion coefficients and viscosities in molecular dynamics simulations under periodic boundary conditions was studied. But the authors focused on the effect of the number of particles in the simulation box.
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Free energy reconstruction from nonequilibrium single-molecule pulling experiments.

TL;DR: It is shown how equilibrium free energy profiles can be extracted rigorously from repeated nonequilibrium force measurements on the basis of an extension of Jarzynski's remarkable identity between free energies and the irreversible work.
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Osmotic water transport through carbon nanotube membranes

TL;DR: The observed flow rates are high, comparable to those through the transmembrane protein aquaporin-1, and are practically independent of the length of the nanotube, in contrast to predictions of macroscopic hydrodynamics.