64 research outputs found

    Wind turbine generator rotor blade concepts with low cost potential

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    Four processed for producing blades are examined. Two use filament winding techniques and two involve filling a mold or form to produce all or part of a blade. The processes are described and a comparison is made of cost, material properties, design and free vibration characteristics. Conclusions are made regarding the feasibility of each process to produce low cost, structurally adequate blades

    Análise morfométrica de tecido muscular de coelhos submetido a ultra-som pulsado e contínuo de 1 MHz I

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    Visando estabelecer uma relação entre os efeitos do ultra-som e a variação da área da célula muscular, este estudo analisou os efeitos do ultra-som (US) de 1 MHz, pulsado e contínuo, utilizado com a intensidade máxima de 3 W/cm2, em tecido muscular sadio do músculo vasto lateral de coelhos (Oryctolagus Cuniculus) machos adultos. Utilizaram-se dois grupos, cada um com 5 coelhos, sendo um para o US pulsado e o outro para o US contínuo. Utilizou-se a coxa esquerda dos coelhos como antímero experimental, sendo a direita o controle. Em ambos os grupos foram realizadas 10 sessões consecutivas de US de 1 MHz, com intensidade de 3 W / c m 2 / durante 12 minutos. Ao término das 10 sessões os coelhos foram sacrificados, retirando-se o músculo vasto lateral, bilateralmente, para preparação das lâminas, que foram analisadas histomorfometricamente. Consideraram-se sempre 10 célulasmusculares em cada extremidade da lâmina analisada - superior, inferior,direita e esquerda. Obtiveram-se assim 40 células analisadas, em cadaantímero de cada coelho. Pela análise estatística (teste t-Student) da média das áreas destas células, verificou-se que não houve diferençasignificativa entre o antímero experimental e o controle em ambos os grupos. Conclui-se que, com a metodologia empregada nesta pesquisa, o US não produz efeitos morfométricos no tecido muscular sadio de coelhos.In order to seek a relation between applied ultrasound (US) and variation of muscle cell area, this study analysed the effects of 1 MHz US, in pulsed and continuous mode, at the maximum intensity of 3 W/cm2, in healthy muscle tissue of adult male rabbits' (Oryctolagus Cuniculus) vast lateral muscle. Rabbits' left thighs were tested in the experiment, the right ones being taken as control. Two groups of 5 rabbits each were formed, one for pulsed U S and the other for continuous US. In both groups were applied 10 consecutive sessions of 1 MHz US with intensity of 3 W/cm2 during 12 minutes. At the end of the 10 sessions the rabbits were sacrificed and both thighs lateral muscles were excised, prepared and fixed to slides for microscopic analysis of the cells area. Ten cells were considered at each slide sector (upper, lower, right and left), thus a total of 40 cells were analysed from each thigh. The mean area of cells for each slide sector was compared to control thigh cells area by means of t-Student test. No statistical I ly significant differences were found between the two sides in both groups, leading to the conclusion that, with the described methodology, US does not produce any effect in the cell size of rabbits healthy muscles

    Improving the performance of DomainDiscovery of protein domain boundary assignment using inter-domain linker index

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    BACKGROUND: Knowledge of protein domain boundaries is critical for the characterisation and understanding of protein function. The ability to identify domains without the knowledge of the structure – by using sequence information only – is an essential step in many types of protein analyses. In this present study, we demonstrate that the performance of DomainDiscovery is improved significantly by including the inter-domain linker index value for domain identification from sequence-based information. Improved DomainDiscovery uses a Support Vector Machine (SVM) approach and a unique training dataset built on the principle of consensus among experts in defining domains in protein structure. The SVM was trained using a PSSM (Position Specific Scoring Matrix), secondary structure, solvent accessibility information and inter-domain linker index to detect possible domain boundaries for a target sequence. RESULTS: Improved DomainDiscovery is compared with other methods by benchmarking against a structurally non-redundant dataset and also CASP5 targets. Improved DomainDiscovery achieves 70% accuracy for domain boundary identification in multi-domains proteins. CONCLUSION: Improved DomainDiscovery compares favourably to the performance of other methods and excels in the identification of domain boundaries for multi-domain proteins as a result of introducing support vector machine with benchmark_2 dataset

    A framework for protein structure classification and identification of novel protein structures

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    BACKGROUND: Protein structure classification plays a central role in understanding the function of a protein molecule with respect to all known proteins in a structure database. With the rapid increase in the number of new protein structures, the need for automated and accurate methods for protein classification is increasingly important. RESULTS: In this paper we present a unified framework for protein structure classification and identification of novel protein structures. The framework consists of a set of components for comparing, classifying, and clustering protein structures. These components allow us to accurately classify proteins into known folds, to detect new protein folds, and to provide a way of clustering the new folds. In our evaluation with SCOP 1.69, our method correctly classifies 86.0%, 87.7%, and 90.5% of new domains at family, superfamily, and fold levels. Furthermore, for protein domains that belong to new domain families, our method is able to produce clusters that closely correspond to the new families in SCOP 1.69. As a result, our method can also be used to suggest new classification groups that contain novel folds. CONCLUSION: We have developed a method called proCC for automatically classifying and clustering domains. The method is effective in classifying new domains and suggesting new domain families, and it is also very efficient. A web site offering access to proCC is freely available a

    Improved general regression network for protein domain boundary prediction

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    Background: Protein domains present some of the most useful information that can be used to understand protein structure and functions. Recent research on protein domain boundary prediction has been mainly based on widely known machine learning techniques, such as Artificial Neural Networks and Support Vector Machines. In this study, we propose a new machine learning model (IGRN) that can achieve accurate and reliable classification, with significantly reduced computations. The IGRN was trained using a PSSM (Position Specific Scoring Matrix), secondary structure, solvent accessibility information and inter-domain linker index to detect possible domain boundaries for a target sequence. Results: The proposed model achieved average prediction accuracy of 67% on the Benchmark_2 dataset for domain boundary identification in multi-domains proteins and showed superior predictive performance and generalisation ability among the most widely used neural network models. With the CASP7 benchmark dataset, it also demonstrated comparable performance to existing domain boundary predictors such as DOMpro, DomPred, DomSSEA, DomCut and DomainDiscovery with 70.10% prediction accuracy. Conclusion: The performance of proposed model has been compared favourably to the performance of other existing machine learning based methods as well as widely known domain boundary predictors on two benchmark datasets and excels in the identification of domain boundaries in terms of model bias, generalisation and computational requirements. © 2008 Yoo et al; licensee BioMed Central Ltd

    Automatic structure classification of small proteins using random forest

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    <p>Abstract</p> <p><b>Background</b></p> <p>Random forest, an ensemble based supervised machine learning algorithm, is used to predict the SCOP structural classification for a target structure, based on the similarity of its structural descriptors to those of a template structure with an equal number of secondary structure elements (SSEs). An initial assessment of random forest is carried out for domains consisting of three SSEs. The usability of random forest in classifying larger domains is demonstrated by applying it to domains consisting of four, five and six SSEs.</p> <p><b>Result</b>s</p> <p>Random forest, trained on SCOP version 1.69, achieves a predictive accuracy of up to 94% on an independent and non-overlapping test set derived from SCOP version 1.73. For classification to the SCOP <it>Class, Fold, Super-family </it>or <it>Family </it>levels, the predictive quality of the model in terms of Matthew's correlation coefficient (MCC) ranged from 0.61 to 0.83. As the number of constituent SSEs increases the MCC for classification to different structural levels decreases.</p> <p>Conclusions</p> <p>The utility of random forest in classifying domains from the place-holder classes of SCOP to the true <it>Class, Fold, Super-family </it>or <it>Family </it>levels is demonstrated. Issues such as introduction of a new structural level in SCOP and the merger of singleton levels can also be addressed using random forest. A real-world scenario is mimicked by predicting the classification for those protein structures from the PDB, which are yet to be assigned to the SCOP classification hierarchy.</p
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