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Particle resolved direct numerical simulation (PR-DNS) has been used extensively to obtain closures for heat transfer from static particle arrays.
The DNA structure from nucleosome core particle resolved by X-ray crystallography was used as a structural template (Davey et al. 2002).
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DOI: http://dx.doi.org/10.7554/eLife.03273.005 The ability to visualize not only DNA binding to the CMG but also the position of the duplex end with respect to the particle, resolves a key question concerning the polarity by which MCM helicases engage a presumptive translocation strand.
In conjunction with a reaction mechanism for iron reduction through carbon monoxide, the spatially and temporarily dependent reduction degree for each individual particle is resolved.
Early-log cultures of E. coli were grown in the presence of 2× MIC of lamotrigine at 15°C in LB media for 5 min, 1 hr, and 6 hr, at which time the ribosomal particles were resolved on sucrose gradients, and the rRNA corresponding to each discrete particle was purified and reverse transcribed using 5′ carboxyfluorescein-tagged primers.
Stained protein gel: 8 μg of particles were resolved by 10% SDS PAGE and thereafter stained overnight with SYPRO Ruby for total protein analysis.
Western blot: 4 μg of particles were resolved on a 10% SDS-PAGE gel and transferred onto a nitrocellulose membrane in Towbin buffer (192 mM glycine, 25 mm Tris, 20% methanol, Thermo Fisher Scientific) for Western blot analysis.
In this approach, the particles are resolved as discrete phase coupled via heat, mass and momentum transfer to the surrounding gas phase.
Second, the locations and orientations of the 3D particles are resolved by a simulated annealing method, which is intrinsically a non-deterministic approach, and thus the optimality is not always guaranteed.
The particles were retained in the stacking region of the gel while all of the captured proteins were electroeluted from particles and resolved in the gel.
Free and SWR1-bound nucleosome core particles were resolved on a 1.3% agarose gel.
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