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1.
Heliyon ; 10(7): e28387, 2024 Apr 15.
Article in English | MEDLINE | ID: mdl-38586371

ABSTRACT

The aim of this study is to explore the characteristics of an active Free-Piston Stirling Engine (AFPSE) through the use of machine learning methods. Due to the time-intensive nature of extracting simulation results from complex thermal equations, an Artificial Neural Network (ANN) is utilized to expedite the process. To construct a nonlinear model, 5000 samples are extracted from simulation results. Input parameters included in the model are the hot and cold source temperatures, the voltage given to the DC motor, spring stiffness, and the mass of the power piston, while output parameters are the amplitude and frequency of power piston displacement. The proposed ANN model structure comprises two hidden layer with 10 and 20 neurons, respectively, indicating the applicability of the ANN model in estimating significant parameters of AFPSE in a shorter amount of time. The firefly optimization algorithm is utilized to determine the unknown input parameters of ANN and maximize the output power. Results indicate that a maximum output power of 23.07 W can be attained by applying 8.5 V voltage on the DC motor. This study highlights the potential of machine learning techniques to explore the primary features of AFPSE.

2.
J Virol ; 79(21): 13385-98, 2005 Nov.
Article in English | MEDLINE | ID: mdl-16227260

ABSTRACT

The complete genomic sequence of kelp fly virus (KFV), originally isolated from the kelp fly, Chaetocoelopa sydneyensis, has been determined. Analyses of its genomic and structural organization and phylogeny show that it belongs to a hitherto undescribed group within the picorna-like virus superfamily. The single-stranded genomic RNA of KFV is 11,035 nucleotides in length and contains a single large open reading frame encoding a polypeptide of 3,436 amino acids with 5' and 3' untranslated regions of 384 and 343 nucleotides, respectively. The predicted amino acid sequence of the polypeptide shows that it has three regions. The N-terminal region contains sequences homologous to the baculoviral inhibitor of apoptosis repeat domain, an inhibitor of apoptosis commonly found in animals and in viruses with double-stranded DNA genomes. The second region contains at least two capsid proteins. The third region has three sequence motifs characteristic of replicase proteins of many plant and animal viruses, including a helicase, a 3C chymotrypsin-like protease, and an RNA-dependent RNA polymerase. Phylogenetic analysis of the replicase motifs shows that KFV forms a distinct and distant taxon within the picorna-like virus superfamily. Cryoelectron microscopy and image reconstruction of KFV to a resolution of 15 A reveals an icosahedral structure, with each of its 12 fivefold vertices forming a turret from the otherwise smooth surface of the 20-A-thick capsid. The architecture of the KFV capsid is unique among the members of the picornavirus superfamily for which structures have previously been determined.


Subject(s)
Diptera/virology , Genome, Viral , Insect Viruses/classification , Picornaviridae/classification , Amino Acid Sequence , Animals , Capsid/chemistry , Capsid/ultrastructure , Capsid Proteins/genetics , Insect Viruses/genetics , Insect Viruses/ultrastructure , Molecular Sequence Data , Open Reading Frames/genetics , Phylogeny , Picornaviridae/genetics , Picornaviridae/ultrastructure , RNA-Dependent RNA Polymerase/genetics , Sequence Alignment , Sequence Analysis
3.
Genetics ; 156(4): 1559-71, 2000 Dec.
Article in English | MEDLINE | ID: mdl-11102357

ABSTRACT

The extracellular proteases of Aspergillus nidulans are produced in response to limitation of carbon, nitrogen, or sulfur, even in the absence of exogenous protein. Mutations in the A. nidulans xprF and xprG genes have been shown to result in elevated levels of extracellular protease in response to carbon limitation. The xprF gene was isolated and sequence analysis indicates that it encodes a 615-amino-acid protein, which represents a new type of fungal hexokinase or hexokinase-like protein. In addition to their catalytic role, hexokinases are thought to be involved in triggering carbon catabolite repression. Sequence analysis of the xprF1 and xprF2 alleles showed that both alleles contain nonsense mutations. No loss of glucose or fructose phosphorylating activity was detected in xprF1 or xprF2 mutants. There are two possible explanations for this observation: (1) the xprF gene may encode a minor hexokinase or (2) the xprF gene may encode a protein with no hexose phosphorylating activity. Genetic evidence suggests that the xprF and xprG genes are involved in the same regulatory pathway. Support for this hypothesis was provided by the identification of a new class of xprG(-) mutation that suppresses the xprF1 mutation and results in a protease-deficient phenotype.


Subject(s)
Aspergillus nidulans/genetics , Endopeptidases/metabolism , Fungal Proteins/genetics , Genes, Fungal , Alleles , Amino Acid Sequence , Arabidopsis/enzymology , Arabidopsis/genetics , Aspergillus nidulans/enzymology , Base Sequence , Chromosome Mapping , Chromosomes, Fungal/genetics , Codon, Nonsense , DNA, Fungal/genetics , Fructose/metabolism , Fungal Proteins/metabolism , Fungal Proteins/physiology , Gene Expression Regulation, Enzymologic , Gene Expression Regulation, Fungal , Glucose/metabolism , Hexokinase/chemistry , Hexokinase/genetics , Humans , Molecular Sequence Data , Phosphorylation , Phylogeny , Plant Proteins/chemistry , Saccharomyces cerevisiae/enzymology , Saccharomyces cerevisiae/genetics , Sequence Alignment , Sequence Homology, Amino Acid , Species Specificity
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