984 resultados para Shape factor
Resumo:
The length-weight relationship and condition factor of Mylopharyngodon spiceus were determined. The result of the study showed the dependence of weight (W) on the total length (L) in the following form: W= 0.006L(super 3.156) or in the logarithmic form Log W=- 2.1851 + 3.156 Log L. Standard errors of length and weight were 0.674 cm and 3.214 g respectively. The co-efficient correlation "r" was found to be 0.972 which indicated that the relationship between length and body weight of the fish was highly significant. The t-test also indicated that the correlation between length and weight was significant. The range and mean value of condition factor (K) were 0.865 to 1.041 and 0.958 respectively.
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A nonparametric Bayesian extension of Factor Analysis (FA) is proposed where observed data $\mathbf{Y}$ is modeled as a linear superposition, $\mathbf{G}$, of a potentially infinite number of hidden factors, $\mathbf{X}$. The Indian Buffet Process (IBP) is used as a prior on $\mathbf{G}$ to incorporate sparsity and to allow the number of latent features to be inferred. The model's utility for modeling gene expression data is investigated using randomly generated data sets based on a known sparse connectivity matrix for E. Coli, and on three biological data sets of increasing complexity.
Resumo:
We consider the robust control of plants with saturation nonlinearities from an input/output viewpoint. First, we present a parameterization for anti-windup control based on coprime factorizations of the controller. Second, we propose a synthesis method which exploits the freedom to choose a particular coprime factorization.
Resumo:
Based on shape memory effect of the sputtered thin film shape memory alloys, different types of micromirror structures were designed and fabricated for optical sensing application. Using surface micromachining, TiNi membrane mirror structure has been fabricated, which can be actuated based on intrinsic two-way shape memory effect of the free-standing TiNi film. Using bulk micromachining, TiNi/Si and TiNi/Si 3N 4microcantilever mirror structures were fabricated. © 2007 IOP Publishing Ltd.
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For Micro-electro-mechanical System (MEMS) applications, TiNi-based thin film Shape Memory Alloys (SMAs) possess many desirable properties, such as high power density, large transformation stress and strain upon heating and cooling, superelasticity and biocompatibility. In this paper, recent development in TiNi-based thin film SMA and microactuator applications is discussed. The topics related to film deposition and characterisation is mainly focused on crystal nucleation and growth during annealing, film thickness effect, film texture, stress induced surface relief, wrinkling and trenches as well as Temperature Memory Effect (TME). The microactuator applications are mainly focused on microvalve and microcage for biological applications, micromirror for optical applications and data storage using nanoindentation method. Copyright © 2009, Inderscience Publishers.
Resumo:
The mixtures of factor analyzers (MFA) model allows data to be modeled as a mixture of Gaussians with a reduced parametrization. We present the formulation of a nonparametric form of the MFA model, the Dirichlet process MFA (DPMFA). The proposed model can be used for density estimation or clustering of high dimensiona data. We utilize the DPMFA for clustering the action potentials of different neurons from extracellular recordings, a problem known as spike sorting. DPMFA model is compared to Dirichlet process mixtures of Gaussians model (DPGMM) which has a higher computational complexity. We show that DPMFA has similar modeling performance in lower dimensions when compared to DPGMM, and is able to work in higher dimensions. ©2009 IEEE.
Resumo:
In this paper, we aim to reconstruct free-from 3D models from a single view by learning the prior knowledge of a specific class of objects. Instead of heuristically proposing specific regularities and defining parametric models as previous research, our shape prior is learned directly from existing 3D models under a framework based on the Gaussian Process Latent Variable Model (GPLVM). The major contributions of the paper include: 1) a probabilistic framework for prior-based reconstruction we propose, which requires no heuristic of the object, and can be easily generalized to handle various categories of 3D objects, and 2) an attempt at automatic reconstruction of more complex 3D shapes, like human bodies, from 2D silhouettes only. Qualitative and quantitative experimental results on both synthetic and real data demonstrate the efficacy of our new approach. ©2009 IEEE.
Resumo:
A specific blood coagulation factor X activator was purified from the venom of Ophiophagus hannah by gel filtration and two steps of FPLC Mono-Q column ion-exchange chromatography. It showed a single protein band both in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and alkaline polyacrylamide gel electrophoresis. The mol. wt was estimated to be 62,000 in non-reducing conditions and 64,500 in reducing conditions by SDS-PAGE. The isoelectric point was found to be pH 5.6. The enzyme had weak amidolytic activities toward CBS 65-25, but it showed no activities on S-2266, S-2302, thrombin substrate S-2238, plasmin substrate S-2251 or factor Xa substrate S-2222. It had no arginine esterase activity toward substrate benzoylarginine ethylester (BAEE). The enzyme activated factor X in vitro and the effect was absolutely Ca2+ dependent, with a Hill coefficient of 6.83. It could not activate prothrombin nor had any effect on fibrinogen and thus appeared to act specifically on factor X. The procoagulant activity of the enzyme was almost completely inhibited by serine protease inhibitors like PMSF, TPCK and soybean trypsin inhibitor; partially inhibited by L-cysteine. Metal chelator EDTA did not inhibit its procoagulant activity. These results suggest that the factor X activator from O. hannah venom is a serine protease.
Resumo:
A specific activator of blood coagulation factor X was purified from the venom of Bungarus fasciatus by gel filtration and by ion-exchange chromatography on a Mono-Q column (FPLC). It consisted of a single polypeptide chain, with a mel. wt of 70,000 in reducing and non-reducing conditions. The enzyme had an amidolytic activity towards the chromogenic substrates S-2266 and S-2302 but it did not hydrolyse S-2238, S2251 or S-2222, which are specific substrates for thrombin, plasmin and factor Xa, respectively. The enzyme activated factor X in vitro and the effect was Ca2+ dependent with a Hill coefficient of 7.9. As with physiological activators, the venom activator cleaves the heavy chain of factor X, producing the activated factor Xa alpha. The purified factor X activator from B. fasciatus venom did not activate prothrombin, nor did it cleave or clot purified fibrinogen. The amidolytic activity and the factor X activation activity of the factor X activator from B. fasciatus venom were readily inhibited by serine protease inhibitors such as diisopropyl fluorophosphate (DFP), phenylmethanesulfonyl fluoride (PMSF), benzamidine and by soybean trypsin inhibitor but not by EDTA. These observations suggest that the factor X activator from B. fasciatus venom is a serine protease. It therefore differs from those of activators obtained from Vipera russelli and Bothrops atrox venoms, which are metalloproteinases.
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A blood coagulation factor IX-binding protein (TSV-FIX-BP) was isolated from the snake venom of Trimeresurus stejnegeri. On SDS-polyacrylamide gel electrophoresis, TSV-FIX-BP showed a single band with an apparent molecular weight of 23,000 under non-reducing conditions. and two distinct bands with apparent molecular weights of 14,800 and 14,000 under reducing conditions. cDNA clones containing the coding sequences of TSV-FIX-BP were isolated and sequenced to determine the structure of the precusors of TSV-FIX-BP subunits. The deduced amino acid sequences of two subunits of TSV-FIX-BP were confirmed by N-terminal protein sequencing and trypsin-digested peptide mass fingerprinting. TSV-FIX-BP was a nonenzymatic C-type lectin-like anti-coagulant. The anti-coagulant activity of TSV-FIX-BP was mainly caused by its dose dependent interaction with blood coagulation factor IX but not with blood coagulation factor X. (C) 2003 Elsevier Science Ltd. All rights reserved.