RCD: Rapid Close to Deadline Scheduling for Datacenter Networks

Datacenter-based Cloud Computing services provide a flexible, scalable and yet economical infrastructure to host online services such as multimedia streaming, email and bulk storage. Many such services perform geo-replication to provide necessary quality of service and reliability to users resulting in frequent large inter- datacenter transfers. In order to meet tenant service level agreements (SLAs), these transfers have to be completed prior to a deadline. In addition, WAN resources are quite scarce and costly, meaning they should be fully utilized. Several recently proposed schemes, such as B4, TEMPUS, and SWAN have focused on improving the utilization of inter-datacenter transfers through centralized scheduling, however, they fail to provide a mechanism to guarantee that admitted requests meet their deadlines. Also, in a recent study, authors propose Amoeba, a system that allows tenants to define deadlines and guarantees that the specified deadlines are met, however, to admit new traffic, the proposed system has to modify the allocation of already admitted transfers. In this paper, we propose Rapid Close to Deadline Scheduling (RCD), a close to deadline traffic allocation technique that is fast and efficient. Through simulations, we show that RCD is up to 15 times faster than Amoeba, provides high link utilization along with deadline guarantees, and is able to make quick decisions on whether a new request can be fully satisfied before its deadline.Comment: World Automation Congress (WAC), IEEE, 201

Studies on carbohydrate moieties of the glycoprotein, glucoamylase II of Aspergillus niger: nature of carbohydrate-peptide linkage and structure of oligosaccharides

Electrophoretically homogeneous type 1 (GP-C1 and GP-C2), type 2 (GP-C3a and GP-C3b,) and type 3 (GP-D1, and GP-D2) glycopeptides from Aspergillus niger glucoamylase II (Manjunath and Raghavendra Rao, preceding paper) were separately treated with alkaline borohydride. The (β-eliminated oligosaccharides were subjected to single and sequential digestion with specific glycosidases and the products analysed by gas liquid chromatography. The studies revealed that carbohydrate moieties were present as mannose, Man-Man-, and trisaccharide structures, namely, (a) GIc-Man-Man-, (b) Gal-Man-Man, (c) Man-Man-Man-, (d) GlcNAc-Man-Man-, and (e) Xyl-Man-Man. None of the glycopeptides contained all the trisaccharide structures (a) to (e). Type 1 glycopeptide contained structures (a), (b) and (c); type 2, (a) and (d) and type 3, (a), (b) and (e). The number of carbohydrate units (mono-, di-and trisaccharides) present in the major glycopeptides was determined and tentative structures for the glycopeptides proposed. Carbohydrate units appeared to occur in clusters of 4 to 7 in each glycopeptide, a structure unique to the carbohydrate moiety in Aspergillus niger glucoamylase. Based on carbohydrate analysis and yields of glycopeptide, the number of units of each type of glycopeptide present in glucoamylase II was tentatively calculated to give two of type Man:Glc:Gal = 12-15:l:l, one of type Man:Glc:GlcN = 10-l1:1:2 and one of type Man :GIc :Gal:Xyl = 4-8:0.1:0.5-0.8:0.3-1 glycopeptides

Comparative studies on glucoamylases from three fungal sources

Five commercial preparations of glucoamylases (three from Aspergillus niger, one each from Aspergillus foetidus and Aspergillus candidus) were purified by ultrafiltration, Sepharose-gel filtration and DEAE-sephadex chromatography. Two forms of the enzyme, namely glucoamylase I and glucoamylase II were obtained from the fungi except from one strain of A. Niger. All the enzymes appeared homogeneous by electrophoresis and ultracentrifugation. The specific activities varied between 85 and 142 units. The pH and temperature optima were between 4 and 5, and 60°C respectively. The molecular weight as determined by the sodium dodecyl sulphate-polyacrylamide gel electrophoresis ranged from 75,000 to 79,000 for glucoamylase I and 60,000 to 72,000 for glucoamylase II. Only A. niger glucoamylases contained phenylalanine at the N-terminal end. The amino acid composition of the enzymes was generally similar. However, A. niger and A. foetidus glucoamylases, in contrast to A. candidus enzymes, contained greater percentage of acidic than of basic amino acids. The enzymes contained 15 to 30% carbohydrate and 49 to 57 residues of monosaccharides per mol. A. niger enzymes contained mannose, glucose, galactose, xylose and glucosamine but the A. candidus enzyme lacked xylose and glucose and only xylose was absent in A, foetidus enzymes. Majority of the carbohydrate moieties were O-glycosidically linked through mannose to the hydroxyl groups of seline and threonine of the polypeptide chain

Excretion of lysine by Micrococcus glutamicus

Analysis of intracellular and extracellular lysine concentration during lysine fermentation by Micrococcus glutamicus AEC RN-13-6/1 indicated that lysine excretion occurs against a concentration gradient towards the end of the fermentation period. The capacity to excrete lysine against a concentration gradient may be a factor contributing to the high yield of lysine

Studies on carbohydrate moieties of Aspergillus niger glucoamylase. II: Isolation, purification and characterization of glycopeptides

Six glycopeptide fractions namely GP-C1, GP-C2, GP-C3a, GP-C3b, GP-D, and GP-D2 were isolated after exhaustive digestion of glucoamylase II (Glucozyme) from Aspergillus niger with pronase. They were purified using gel-filtration. high-voltage paper electrophoresis and ion-exchange chromatography on Dowex-50 and Dowex-1. They appeared homogeneous on electrophoresis under different conditions of pHs. The molecular weights ranged from 1600 and 4000 for these glycopeptides. Ally of them contained serine at the N-terminal end. Serine and threonine were the major amino acids with glycine, alanine, proline and tryosine present as minor constituents. Carbohydrate analysis revealed the presence of different sugars. Based on this, the glycopeptides were grouped into three types: (1) GP-C1 and GP-C2 containing mannose, glucose and galactose; (2) GP-C3a, and GP-C3b,containing mannose glucose and glucosamine; and (3) GP-D1 and GP-D2, containing mannose. glucose, galactose and xylose. Most sugar constituents in each glycopeptide occured in non-integral ratios implying a microheterogeneity of the carbohydrate moiety in Aspergillus niger glucoamylase II

Finite Element Magnetostatic Analysis of Magnetostrictive (Tb0.3Dy0.7Fe1.95) Actuator with Different Housing Materials

Permeability of a housing material is one of the significant factors affecting the performance of Tb0.3Dy0.7Fe1.95 based magnetostrictive actuator. According to Lenz’s law the rate of flux transfer depends on permeability of housing material surrounding the terfenol-D. In this paper the co-axial coils in a free air are analysed under direct current excitation and the results are found to agree well with both analytical and Maxwell simulation. Also, the comparison of flux density distribution in co-axial coils placed inside different housing materials of magnetostrictive actuator is found by solving magnetostatic equations using Ansoft Maxwell 2D solver. The axial distribution of magnetic flux density, radial distribution of magnetic flux density and flux distribution in the actuator assembly with different housing materials namely mild steel, cast iron and aluminium with and without Terfenol-D are discussed.Defence Science Journal, 2013, 63(4), pp.423-428, DOI:http://dx.doi.org/10.14429/dsj.63.486

Isomorphism testing of read-once functions and polynomials

In this paper, we study the isomorphism testing problem of formulas in the Boolean and arithmetic settings. We show that isomorphism testing of Boolean formulas in which a variable is read at most once (known as read-once formulas) is complete for log-space. In contrast, we observe that the problem becomes polynomial time equivalent to the graph isomorphism problem, when the input formulas can be represented as OR of two or more monotone read-once formulas. This classifies the complexity of the problem in terms of the number of reads, as read-3 formula isomorphism problem is hard for coNP. We address the polynomial isomorphism problem, a special case of polynomial equivalence problem which in turn is important from a cryptographic perspective[Patarin EUROCRYPT\u2796, and Kayal SODA\u2711]. As our main result, we propose a deterministic polynomial time canonization scheme for polynomials computed by constant-free read-once arithmetic formulas. In contrast, we show that when the arithmetic formula is allowed to read a variable twice, this problem is as hard as the graph isomorphism problem

Structure and stability of glucoamylase II from Aspergillus niger: a circular dichroism study

Glucoamylase II (EC 3.2.1.3) from Aspergillus niger has 31 % α-helix, 36 % β-structure and rest aperiodic structure at pH 4.8 as analysed by the method of Provencher and Glockner (1981,Biochemistry, 20,33). In the near ultra-violet circular dichroism spectrum the enzyme exhibits peaks at 304, 289, 282 and 257 nm and troughs at 285, 277 and 265 nm respectively. The enzyme activity and structure showed greater stability at pH 4.8 than at pH 7.0, were highly sensitive to alkaline pH but less sensitive to acid pH values. The enzyme retained most of its catalytic activity and structure even on partial removal of carbohydrate moieties by periodate treatment but was less stable at higher temperatures and storage at 30‡C. Reduction of the periodate treated enzyme did not reverse the loss of stability. Binding of the synthetic substrate, p-nitrophenyl-α-D-glucoside, perturbed the environment around aromatic amino acids and caused a decrease in the ordered structure