Universal Decimal Classification : a Unique Scheme with its Origin,Development and Credibility

this article deals with the emergence, background history and usages of the Universal Decimal Classification scheme(UDC).It also speaks about the influence of the very scheme over different languages in different countries.It focuses also on the scheme’s acceptability and flexibility to the universal users.This article discusses the scheme’s inclination to be transformed into a machine readable version to compete with other schemes full-fledgedly.Here, the significance of classification scheme in a multilingual atmosphere  is highlighted and future advancements delineated

Stereometric Design for Desk-Top SFF Fabrication

Solid Freeform Fabrication (SFF) technologies refer to the fabrication of physical parts directly from computer based solid models described by STL (Stereo Lithography) or VRML (Virtual Reality Modeling Language) files generated by Computer-Aided Design (CAD) systems. Most of the SFF processes produce parts by building them layer by layer using a row by row pattern, though it is possible to build the part using other patterns. The SFF technology represents a challenge to designers who, in addition to making decisions concerning optimum shape and functionality of the entire part, have'to take under consideration several other manufacturing factors. These factors cover a wide range of technical issues such as Computer-Aided Design model generation, part description and model slicing files, laser path files, precision of part design, rendering patterns, manufacturing tolerances, thermal expansion and residual stress phenomena. This paper investigates the effect of rendering patterns on the integrity, material characteristics and mechanical properties of the parts prepared by a desk-top SFF device using diode lasers. Fe - Bronze (Cu - Sn) premixed metal powders were used as the starting material. The particle size was about 100 /lm to 200 /lm. Density, tensile strength and microstructure of the parts prepared using different rendering patterns were characterized. The results were analyzed to seek optimal rendering patterns. It was noticed that the samples were strong along the laser scanning direction, while they were weak perpendicular to the scanning direction. These results suggest that the laser scanning patterns should be designed to minimize the warping and maximize the strength of the part in the direction depending on the part's function.Mechanical Engineerin

Mechanism of amyloid β-protein dimerization determined using single-molecule AFM force spectroscopy.

Aβ42 and Aβ40 are the two primary alloforms of human amyloid β-protein (Aβ). The two additional C-terminal residues of Aβ42 result in elevated neurotoxicity compared with Aβ40, but the molecular mechanism underlying this effect remains unclear. Here, we used single-molecule force microscopy to characterize interpeptide interactions for Aβ42 and Aβ40 and corresponding mutants. We discovered a dramatic difference in the interaction patterns of Aβ42 and Aβ40 monomers within dimers. Although the sequence difference between the two peptides is at the C-termini, the N-terminal segment plays a key role in the peptide interaction in the dimers. This is an unexpected finding as N-terminal was considered as disordered segment with no effect on the Aβ peptide aggregation. These novel properties of Aβ proteins suggests that the stabilization of N-terminal interactions is a switch in redirecting of amyloids form the neurotoxic aggregation pathway, opening a novel avenue for the disease preventions and treatments

Mechanism of amyloid β-protein dimerization determined using single-molecule AFM force spectroscopy.

Aβ42 and Aβ40 are the two primary alloforms of human amyloid β-protein (Aβ). The two additional C-terminal residues of Aβ42 result in elevated neurotoxicity compared with Aβ40, but the molecular mechanism underlying this effect remains unclear. Here, we used single-molecule force microscopy to characterize interpeptide interactions for Aβ42 and Aβ40 and corresponding mutants. We discovered a dramatic difference in the interaction patterns of Aβ42 and Aβ40 monomers within dimers. Although the sequence difference between the two peptides is at the C-termini, the N-terminal segment plays a key role in the peptide interaction in the dimers. This is an unexpected finding as N-terminal was considered as disordered segment with no effect on the Aβ peptide aggregation. These novel properties of Aβ proteins suggests that the stabilization of N-terminal interactions is a switch in redirecting of amyloids form the neurotoxic aggregation pathway, opening a novel avenue for the disease preventions and treatments