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1.
Percept Mot Skills ; 108(2): 524-30, 2009 Apr.
Artigo em Inglês | MEDLINE | ID: mdl-19544957

RESUMO

The strength of five working muscle groups of the lower arms of 8 male fencers, including adductor pollicis, extensor carpi radialis, flexor carpi radialis, extensor carpi ulnaris, and flexor carpi ulnaris, were examined during competition. Root mean square values of muscular electromyographic signals indicated that the shape of foil handles significantly influenced distribution of working strength of each muscle group. Use of the Pistol-Viscounti type of foil handle showed better distribution of strength among the 5 muscle groups than did other types of foils. Using the Pistol-Viscounti foil handle not only reduced muscular fatigue but also lessened cumulative trauma symptoms while holding a foil for a long duration.


Assuntos
Antebraço/fisiologia , Força da Mão/fisiologia , Força Muscular/fisiologia , Músculo Esquelético/fisiologia , Equipamentos Esportivos/normas , Adulto , Traumatismos em Atletas/prevenção & controle , Fenômenos Biomecânicos/fisiologia , Comportamento Competitivo/fisiologia , Transtornos Traumáticos Cumulativos/prevenção & controle , Desenho de Equipamento/métodos , Humanos , Masculino , Contração Muscular/fisiologia , Fadiga Muscular/fisiologia
2.
IEEE Trans Nanobioscience ; 6(2): 186-96, 2007 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-17695755

RESUMO

The classification of protein structures is essential for their function determination in bioinformatics. At present, a reasonably high rate of prediction accuracy has been achieved in classifying proteins into four classes in the SCOP database according to their primary amino acid sequences. However, for further classification into fine-grained folding categories, especially when the number of possible folding patterns as those defined in the SCOP database is large, it is still quite a challenge. In our previous work, we have proposed a two-level classification strategy called hierarchical learning architecture (HLA) using neural networks and two indirect coding features to differentiate proteins according to their classes and folding patterns, which achieved an accuracy rate of 65.5%. In this paper, we use a combinatorial fusion technique to facilitate feature selection and combination for improving predictive accuracy in protein structure classification. When applying various criteria in combinatorial fusion to the protein fold prediction approach using neural networks with HLA and the radial basis function network (RBFN), the resulting classification has an overall prediction accuracy rate of 87% for four classes and 69.6% for 27 folding categories. These rates are significantly higher than the accuracy rate of 56.5% previously obtained by Ding and Dubchak. Our results demonstrate that data fusion is a viable method for feature selection and combination in the prediction and classification of protein structure.


Assuntos
Algoritmos , Modelos Químicos , Modelos Moleculares , Reconhecimento Automatizado de Padrão/métodos , Proteínas/química , Proteínas/ultraestrutura , Análise de Sequência de Proteína/métodos , Inteligência Artificial , Simulação por Computador , Bases de Dados de Proteínas , Armazenamento e Recuperação da Informação/métodos , Proteínas/classificação , Reprodutibilidade dos Testes , Sensibilidade e Especificidade
3.
Int J Neural Syst ; 15(1-2): 71-84, 2005.
Artigo em Inglês | MEDLINE | ID: mdl-15912584

RESUMO

Over one-third of protein structures contain metal ions, which are the necessary elements in life systems. Traditionally, structural biologists were used to investigate properties of metalloproteins (proteins which bind with metal ions) by physical means and interpreting the function formation and reaction mechanism of enzyme by their structures and observations from experiments in vitro. Most of proteins have primary structures (amino acid sequence information) only; however, the 3-dimension structures are not always available. In this paper, a direct analysis method is proposed to predict the protein metal-binding amino acid residues from its sequence information only by neural networks with sliding window-based feature extraction and biological feature encoding techniques. In four major bulk elements (Calcium, Potassium, Magnesium, and Sodium), the metal-binding residues are identified by the proposed method with higher than 90% sensitivity and very good accuracy under 5-fold cross validation. With such promising results, it can be extended and used as a powerful methodology for metal-binding characterization from rapidly increasing protein sequences in the future.


Assuntos
Simulação por Computador , Metaloproteínas/química , Modelos Moleculares , Redes Neurais de Computação , Conformação Proteica , Sequência de Aminoácidos , Animais , Sítios de Ligação , Bases de Dados de Proteínas , Humanos , Dados de Sequência Molecular , Sensibilidade e Especificidade
4.
IEEE Trans Nanobioscience ; 2(4): 221-32, 2003 Dec.
Artigo em Inglês | MEDLINE | ID: mdl-15376912

RESUMO

The structure classification of proteins plays a very important role in bioinformatics, since the relationships and characteristics among those known proteins can be exploited to predict the structure of new proteins. The success of a classification system depends heavily on two things: the tools being used and the features considered. For the bioinformatics applications, the role of appropriate features has not been paid adequate importance. In this investigation we use three novel ideas for multiclass protein fold classification. First, we use the gating neural network, where each input node is associated with a gate. This network can select important features in an online manner when the learning goes on. At the beginning of the training, all gates are almost closed, i.e., no feature is allowed to enter the network. Through the training, gates corresponding to good features are completely opened while gates corresponding to bad features are closed more tightly, and some gates may be partially open. The second novel idea is to use a hierarchical learning architecture (HLA). The classifier in the first level of HLA classifies the protein features into four major classes: all alpha, all beta, alpha + beta, and alpha/beta. And in the next level we have another set of classifiers, which further classifies the protein features into 27 folds. The third novel idea is to induce the indirect coding features from the amino-acid composition sequence of proteins based on the N-gram concept. This provides us with more representative and discriminative new local features of protein sequences for multiclass protein fold classification. The proposed HLA with new indirect coding features increases the protein fold classification accuracy by about 12%. Moreover, the gating neural network is found to reduce the number of features drastically. Using only half of the original features selected by the gating neural network can reach comparable test accuracy as that using all the original features. The gating mechanism also helps us to get a better insight into the folding process of proteins. For example, tracking the evolution of different gates we can find which characteristics (features) of the data are more important for the folding process. And, of course, it also reduces the computation time.


Assuntos
Algoritmos , Inteligência Artificial , Reconhecimento Automatizado de Padrão , Proteínas/química , Proteínas/classificação , Alinhamento de Sequência/métodos , Análise de Sequência de Proteína/métodos , Sequência de Aminoácidos , Análise por Conglomerados , Metodologias Computacionais , Dados de Sequência Molecular , Redes Neurais de Computação , Conformação Proteica , Dobramento de Proteína , Reprodutibilidade dos Testes , Robótica/métodos , Sensibilidade e Especificidade , Homologia de Sequência de Aminoácidos
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