There is, I think, something ethereal about i —the square root of minus one. I remember first hearing about it at school. It seemed an odd beast at that time—an intruder hovering on the edge of reality.

Usually familiarity dulls this sense of the bizarre, but in the case of i it was the reverse: over the years the sense of its surreal nature intensified. It seemed that it was impossible to write mathematics that described the real world in …

I and i

Three parallel algorithms for classical molecular dynamics are presented. The first assigns each processor a fixed subset of atoms; the second assigns each a fixed subset of inter-atomic forces to compute; the third assigns each a fixed spatial region. The algorithms are suitable for molecular dynamics models which can be difficult to parallelize efficiently—those with short-range forces where the neighbors of each atom change rapidly. They can be implemented on any distributed-memory parallel machine which allows for message-passing of data between independently executing processors. The algorithms are tested on a standard Lennard-Jones benchmark problem for system sizes ranging from 500 to 100,000,000 atoms on several parallel supercomputers--the nCUBE 2, Intel iPSC/860 and Paragon, and Cray T3D. Comparing the results to the fastest reported vectorized Cray Y-MP and C90 algorithm shows that the current generation of parallel machines is competitive with conventional vector supercomputers even for small problems. For large problems, the spatial algorithm achieves parallel efficiencies of 90% and a 1840-node Intel Paragon performs up to 165 faster than a single Cray C9O processor. Trade-offs between the three algorithms and guidelines for adapting them to more complex molecular dynamics simulations are also discussed.

Fast parallel algorithms for short-range molecular dynamics

抗原变异可使得多种致病微生物易于逃避宿主免疫应答。表达在感染红细胞表面的恶性疟原虫红细胞表面蛋白1（PfPMP1）与感染红细胞、内皮细胞、树突状细胞以及胎盘的单个或多个受体作用，在黏附及免疫逃避中起关键的作用。每个单倍体基因组var基因家族编码约60种成员，通过启动转录不同的var基因变异体为抗原变异提供了分子基础。

疟原虫var基因转换速率变化导致抗原变异[英]／Paul H, Robert P, Christodoulou Z, et al//Proc Natl Acad Sci U S A

http://wwwcourses.sens.buffalo.edu/ce435/Riess03.pdf

Micellization of block copolymers

1: Magnetic Particles: Preparation, Properties and Applications: M. Ozaki. 2: Maghemite (gamma-Fe2O3): A Versatile Magnetic Colloidal Material C.J. Serna, M.P. Morales. 3: Dynamics of Adsorption and Oxidation of Organic Molecules on Illuminated Titanium Dioxide Particles Immersed in Water M.A. Blesa, R.J. Candal, S.A. Bilmes. 4: Colloidal Aggregation in Two-Dimensions A. Moncho-Jorda, F. Martinez-Lopez, M.A. Cabrerizo-Vilchez, R. Hidalgo Alvarez, M. Quesada-PMerez. 5: Kinetics of Particle and Protein Adsorption Z. Adamczyk.

Surface and Colloid Science

Up gradation of Small Angle Neutron Scattering (SANS) instrument at Dhruva reactor is carried out through indigenously developed high efficiency 1-dimensional Position Sensitive Detectors (1D PSD) and arranging them in a 2-D structure. The design of PSDs is customized for SANS instrument at Guide Tube Lab Dhruva reactor. Performance of PSDs is comparable to the commercially available ones, in terms of position resolution and neutron detection efficiency, whereas show an advantage of larger detection angle. The multi-PSD structure enhances the efficiency of SANS instrument, allows access to smaller Q, i.e. larger length scales, broader accessible Q range and improved data quality. Design aspects, fabrication details and performance of these PSDs are presented in the paper.

High efficiency 1D position sensitive neutron detectors in fan like 2D structure for SANS instrument at Dhruva

SANS study of Cqm1 protein solution

Interactions of anionic silica nanoparticles with anionic, cationic and nonionic surfactants have directly been studied by contrast variation small angle neutron scattering (SANS). The measurements are performed on 1 wt% of both silica nanoparticles and surfactants of anionic sodium dodecyle sulphate (SDS), cationic dodecyltrimethyl ammonium bromide (DTAB) and non‐ionic polyoxyethylene 10 lauryl ether (C12E10) in aqueous solution. We show that there is no direct interaction in the case of SDS with silica particles, whereas strong interaction for DTAB leads to the aggregation of silica particles. The interaction of C12E10 is found through the micelles adsorbed on the silica particles.

Direct Observation Of Nanoparticle‐Surfactant Interactions Using Small Angle Neutron Scattering

Small-angle neutron scattering has been used to study the interaction of silica nanoparticle with Bovine Serum Albumin (BSA) protein without and with a protein denaturing agent urea. The measurements have been carried out at pH 7 where both the components (nanoparticle and protein) are similarly charged. We show that the interactions in nanoparticle-protein system can be modified by changing the conformation of protein through the presence of urea. In the absence of urea, the strong electrostatic repulsion between the nanoparticle and protein prevents protein adsorption on nanoparticle surface. This non-adsorption, in turn gives rise to depletion attraction between nanoparticles. However, with addition of urea the depletion attraction is completely suppressed. Urea driven denaturation of protein is utilized to expose the positively charged patched of the BSA molecules which eventually leads to adsorption of BSA on nanoparticles eliminating the depletion interaction.

/pdf/modifications-in-nanoparticle-protein-interactions-by-1vc4yjkrb7.pdf

Modifications in nanoparticle-protein interactions by varying the protein conformation

Small‐angle neutron scattering (SANS) and dynamic light scattering (DLS) have been used to study conformational changes in protein bovine serum albumin (BSA) during its unfolding in presence of protein denaturating agents urea and surfactant. On addition of urea, the BSA protein unfolds for urea concentrations greater than 4 M and acquires a random coil configuration with its radius of gyration increasing with urea concentration. The addition of surfactant unfolds the protein by the formation of micelle‐like aggregates of surfactants along the unfolded polypeptide chains of the protein. The fractal dimension of such a protein‐surfactant complex decreases and the overall size of the complex increases on increasing the surfactant concentration. The conformation of the unfolded protein in the complex has been determined directly using contrast variation SANS measurements by contrast matching the surfactant to the medium. Results of DLS measurements are found to be in good agreement with those obtained using SANS.

/pdf/sans-and-dls-studies-of-protein-unfolding-in-presence-of-2d32puqm9i.pdf

SANS and DLS Studies of Protein Unfolding in Presence of Urea and Surfactant

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