D
David A. Kessler
Researcher at United States Naval Research Laboratory
Publications - 378
Citations - 10682
David A. Kessler is an academic researcher from United States Naval Research Laboratory. The author has contributed to research in topics: Population & Instability. The author has an hindex of 46, co-authored 364 publications receiving 9669 citations. Previous affiliations of David A. Kessler include University of Michigan & Lawrence Berkeley National Laboratory.
Papers
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Growth velocity of three-dimensional dendritic crystals.
David A. Kessler,Herbert Levine +1 more
TL;DR: In this article, the shape and growth velocity of 3D dendritic crystals in cubically anisotropic materials were studied and the mechanism of microscopic solvability was used to find a unique needle-crystal solution of the equations of thermal diffusion-controlled solidification.
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Steady-state cracks in viscoelastic lattice models.
David A. Kessler,Herbert Levine +1 more
TL;DR: The introduction of a Kelvin viscosity eta allows for a direct comparison between lattice results and continuum treatments, and this comparison is explored as a function of the driving displacement Delta and the number of transverse rows N.
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Dynamical scaling of the surface of finite-density ballistic aggregation
TL;DR: The roughness of aggregates that are formed by ballistic deposition with nonzero flux density of incoming particles is studied and a relation between the width of the geometrical boundary of the aggregate and thewidth of the active region of growth is derived.
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Mechanical bounds to transcriptional noise.
TL;DR: A simple phenomenological model is presented that is able to incorporate the traditional view of gene expression within a framework with mechanical limits to transcription, and a lower limit of intrinsic noise for any mean expression level is found.
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Mechanisms of cooperativity underlying sequence-independent β-sheet formation
TL;DR: The results suggest that solvation dynamics together with the H-bond angular dependence gives rise to a generic cooperativity in this class of systems; this result explains why pathological aggregates involving β-sheet cores can form from many different proteins.