arXiv subjects

Oliver G. Harlen

Publications and source records attributed to Oliver G. Harlen.

3 recordsLinked to original sources

arXiv2021

Morphologies and dynamics of micro-droplet impact onto an idealised scratch

As inkjet technology develops to produce smaller droplets, substrate features such as accidental scratches or manufacturing defects can potentially affect the outcome of printing, particularly for printed electronics where continuous tracks are required. Here, the deposition of micro-droplets onto a scratch of commensurate size is studied. The scratch is considered as a groove of rectangular cross-section, with rectangular side ridges representing material displaced from the substrate, and seven equilibrium morphologies are identified as a result of inertial spreading, contact-line pinning, imbibition into the scratch and capillary flow. A regime map is constructed in terms of scratch depth and width, and theoretical estimates of the regime boundaries are developed by adapting droplet spreading laws for flat surfaces to account for liquid entering the scratches. Good agreement is seen with numerical results obtained using a GPU-accelerated three-dimensional multiphase lattice Boltzmann model validated against published experiments, and the influences of Reynolds number, Weber number and advancing and receding contact angles are explored. Negative and positive implications of the results for printing applications are discussed and illustrated via multiple-droplet simulations of printing across and along scratches.

physics.flu-dyn↗

arXiv2019

Combined force-torque spectroscopy of proteins by means of multiscale molecular simulation

Assessing the structural properties of large proteins is important to gain an understanding of their function in, e.g., biological systems or biomedical applications. We propose a method to examine the mechanical properties of proteins subject to applied forces by means of multiscale simulation. We consider both stretching and torsional forces, which can be applied independently of each other. We apply torsional forces to a coarse-grained continuum model of the antibody protein immunoglobulin G (IgG) using Fluctuating Finite Element Analysis and identify the area of strongest deformation. This region is essential to the torsional properties of the molecule as a whole, as it represents the softest, most deformable domain. We subject this part of the molecule to torques and stretching forces on an atomistic level, using molecular dynamics simulations, in order to investigate its torsional properties. We calculate the torsional resistance as a function of the rotation of the domain, while subjecting it to various stretching forces. We learn how these obtained torsion profiles evolve with increasing stretching force and show that they exhibit torsion stiffening, which is in qualitative agreement with experimental findings. We argue that combining the torsion profiles for various stretching forces effectively results in a combined force-torque spectroscopy analysis, which may serve as a mechanical signature for the examined molecule.

physics.bio-ph↗

arXiv2012

A Stochastic Finite Element Model for the Dynamics of Globular Macromolecules

We describe a novel coarse-grained simulation method for modelling the dynamics of globular macromolecules, such as proteins. The macromolecule is treated as a continuum that is subject to thermal fluctuations. The model includes a non-linear treatment of elasticity and viscosity with thermal noise that is solved using finite element analysis. We have validated the method by demonstrating that the model provides average kinetic and potential energies that are in agreement with the classical equipartition theorem. In addition, we have performed Fourier analysis on the simulation trajectories obtained for a series of linear beams to confirm that the correct average energies are present in the first two Fourier bending modes. We have then used the new modelling method to simulate the thermal fluctuations of a representative protein over 500ns timescales. Using reasonable parameters for the material properties, we have demonstrated that the overall deformation of the biomolecule is consistent with the results obtained for proteins in general from atomistic molecular dynamics simulations.

physics.comp-ph↗