Browsing by Author "Ho, Shinn-Jang"
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Item type:Item, A novel intelligent multiobjective simulated annealing algorithm for designing robust PID controllers(2008-03-01) ;Hung, Ming-Hao ;Shu, Li-Sun ;Ho, Shinn-Jang ;Hwang, Shiow-FenHo, Shinn-YingThis paper proposes an intelligent multiobjective simulated annealing algorithm (IMOSA) and its application to an optimal proportional integral derivative (PID) controller design problem. A well-designed PID-type controller should satisfy the following objectives: 1) disturbance attenuation; 2) robust stability; and 3) accurate setpoint tracking. The optimal PID controller design problem is a large-scale multiobjective optimization problem characterized by the following: 1) nonlinear multimodal search space; 2) large-scale search space; 3) three tight constraints; 4) multiple objectives; and 5) expensive objective function evaluations. In contrast to existing multiobjective algorithms of simulated annealing, the high performance in IMOSA arises mainly from a novel multiobjective generation mechanism using a Pareto-based scoring function without using heuristics. The multiobjective generation mechanism operates on a high-score nondominated solution using a systematic reasoning method based on an orthogonal experimental design, which exploits its neighborhood to economically generate a set of well-distributed nondominated solutions by, considering individual and overall objectives. IMOSA is evaluated by using a practical design example of a super-maneuverable fighter aircraft system. An efficient existing multiobjective algorithm, the improved strength Pareto evolutionary algorithm, is also applied to the same example for comparison. Simulation results demonstrate high performance of the IMOSA-based method in designing robust PID controllers.Item type:Item, FRKAS: Knowledge Acquisition Using a Fuzzy Rule Base Approach to Insight of DNA-Binding Domains/Proteins(2013-03-01) ;Huang, Hui-Ling ;Chang, Fang-Lin ;Ho, Shinn-Jang ;Shu, Li-SunHuang, Wen-LinNumerous prediction methods of DNA-binding domains/proteins were proposed by identifying informative features and designing effective classifiers. These researches reveal that the DNA-protein binding mechanism is complicated and existing accurate predictors such as support vector machine (SVM) with position specific scoring matrices (PSSMs) are regarded as black-box methods which are not easily interpretable for biologists. In this study, we propose an ensemble fuzzy rule base classifier consisting of a set of interpretable fuzzy rule classifiers (iFRCs) using informative physicochemical properties as features. In designing iFRCs, feature selection, membership function design, and fuzzy rule base generation are all simultaneously optimized using an intelligent genetic algorithm (IGA). IGA maximizes prediction accuracy, minimizes the number of features selected, and minimizes the number of fuzzy rules to generate an accurate and concise fuzzy rule base. Benchmark datasets of DNA-binding domains are used to evaluate the proposed ensemble classifier of 30 iFRCs. Each iFRC has a mean test accuracy of 77.46%, and the ensemble classifier has a test accuracy of 83.33%, where the method of SVM with PSSMs has the accuracy of 82.81%. The physicochemical properties of the first two ranks according to their contribution are positive charge and Van Der Waals volume. Charge complementarity between protein and DNA is thought to be important in the first step of recognition between protein and DNA. The amino acid residues of binding peptides have larger Van Der Waals volumes and positive charges than those of non-binding ones. The proposed knowledge acquisition method by establishing a fuzzy rule-based classifier can also be applicable to predict and analyze other protein functions from sequences.Item type:Item, Inferring S-system Models of Genetic Networks from a Time-series Real Data Set of Gene Expression Profiles(2008) ;Huang, Hui-Ling ;Chen, Kuan-Wei ;Ho, Shinn-Jang ;Ho, Shinn-Ying生物科技學系It is desirable to infer cellular dynamic regulation networks from gene expression profiles to discover more delicate and substantial functions in molecular biology, biochemistry, bioengineering, and pharmaceutics. The S-system model is suitable to characterize biochemical network systems and capable of analyzing the regulatory system dynamics. To cope with the problem "multiplicity of solutions", a sufficient amount of data sets of time-series gene expression profiles were often used. An efficient newly-developed method iTEA was proposed to effectively obtain S-system models from a large number (e.g., 15) of simulated data sets with/without noise. In this study, we propose an extended optimization method (named iTEAP) based on iTEA to infer the S-system models of genetic networks from a time-series real data set of gene expression profiles (using SOS DNA microarray data in E. coli as an example). The algorithm iTEAP generated additionally multiple data sets of gene expression profiles by perturbing the given data set. The results reveal that 1) iTEAP can obtain S-system models with high-quality profiles to best fit the observed profiles; 2) the performance of using multiple data sets is better than that of using a single data set in terms of solution quality, and 3) the effectiveness of iTEAP using a single data set is close to that of iTEA using two real data sets.Item type:Item, OPSO: Orthogonal particle swarm optimization and its application to task assignment problems(2008-03-01) ;Ho, Shinn-Ying ;Lin, Hung-Sui ;Liauh, Weei-Hurng ;Ho, Shinn-Jang生物科技學系This paper proposes a novel variant of particle swarm optimization (PSO), named orthogonal PSO (OPSO), for solving intractable large parameter optimization problems. The standard version of PSO is associated with the lack of a mechanism responsible for the process of high-dimensional vector spaces. The high performance of OPSO arises mainly from a novel move behavior using an intelligent move mechanism (IMM) which applies orthogonal experimental design to adjust a velocity for each particle by using a systematic reasoning method instead of the conventional generate-and-go method. The IMM uses a divide-and-conquer approach to cope with the curse of dimensionality in determining the next move of particles. It is shown empirically that the OPSO performs well in solving parametric benchmark functions and a task assignment problem which is NP-complete compared with the standard PSO with the conventional move behavior. The OPSO with IMM is more specialized than the PSO and performs well on large-scale parameter optimization problems with few interactions between variables.Item type:Item, Predicting and analyzing DNA-binding domains using a systematic approach to identifying a set of informative physicochemical and biochemical properties(2011-02-15) ;Huang, Hui-Lin ;Lin, I-Che ;Liou, Yi-Fan ;Tsai, Chia-TaHsu, Kai-TiBackground: Existing methods of predicting DNA-binding proteins used valuable features of physicochemical properties to design support vector machine (SVM) based classifiers. Generally, selection of physicochemical properties and determination of their corresponding feature vectors rely mainly on known properties of binding mechanism and experience of designers. However, there exists a troublesome problem for designers that some different physicochemical properties have similar vectors of representing 20 amino acids and some closely related physicochemical properties have dissimilar vectors. Results: This study proposes a systematic approach (named Auto-IDPCPs) to automatically identify a set of physicochemical and biochemical properties in the AAindex database to design SVM-based classifiers for predicting and analyzing DNA-binding domains/proteins. Auto-IDPCPs consists of 1) clustering 531 amino acid indices in AAindex into 20 clusters using a fuzzy c-means algorithm, 2) utilizing an efficient genetic algorithm based optimization method IBCGA to select an informative feature set of size m to represent sequences, and 3) analyzing the selected features to identify related physicochemical properties which may affect the binding mechanism of DNA-binding domains/proteins. The proposed Auto-IDPCPs identified m=22 features of properties belonging to five clusters for predicting DNA-binding domains with a five-fold cross-validation accuracy of 87.12%, which is promising compared with the accuracy of 86.62% of the existing method PSSM-400. For predicting DNA-binding sequences, the accuracy of 75.50% was obtained using m=28 features, where PSSM-400 has an accuracy of 74.22%. Auto-IDPCPs and PSSM-400 have accuracies of 80.73% and 82.81%, respectively, applied to an independent test data set of DNA-binding domains. Some typical physicochemical properties discovered are hydrophobicity, secondary structure, charge, solvent accessibility, polarity, flexibility, normalized Van Der Waals volume, pK (pK-C, pK-N, pK-COOH and pK-a(RCOOH)), etc. Conclusions: The proposed approach Auto-IDPCPs would help designers to investigate informative physicochemical and biochemical properties by considering both prediction accuracy and analysis of binding mechanism simultaneously. The approach Auto-IDPCPs can be also applicable to predict and analyze other protein functions from sequences.Item type:Item, Prediction and analysis of protein solubility using a novel scoring card method with dipeptide composition(2012-12-13) ;Huang, Hui-Ling ;Charoenkwan, Phasit ;Kao, Te-Fen ;Lee, Hua-ChinChang, Fang-LinBackground: Existing methods for predicting protein solubility on overexpression in Escherichia coli advance performance by using ensemble classifiers such as two-stage support vector machine (SVM) based classifiers and a number of feature types such as physicochemical properties, amino acid and dipeptide composition, accompanied with feature selection. It is desirable to develop a simple and easily interpretable method for predicting protein solubility, compared to existing complex SVM-based methods. Results: This study proposes a novel scoring card method (SCM) by using dipeptide composition only to estimate solubility scores of sequences for predicting protein solubility. SCM calculates the propensities of 400 individual dipeptides to be soluble using statistic discrimination between soluble and insoluble proteins of a training data set. Consequently, the propensity scores of all dipeptides are further optimized using an intelligent genetic algorithm. The solubility score of a sequence is determined by the weighted sum of all propensity scores and dipeptide composition. To evaluate SCM by performance comparisons, four data sets with different sizes and variation degrees of experimental conditions were used. The results show that the simple method SCM with interpretable propensities of dipeptides has promising performance, compared with existing SVM-based ensemble methods with a number of feature types. Furthermore, the propensities of dipeptides and solubility scores of sequences can provide insights to protein solubility. For example, the analysis of dipeptide scores shows high propensity of a-helix structure and thermophilic proteins to be soluble. Conclusions: The propensities of individual dipeptides to be soluble are varied for proteins under altered experimental conditions. For accurately predicting protein solubility using SCM, it is better to customize the score card of dipeptide propensities by using a training data set under the same specified experimental conditions. The proposed method SCM with solubility scores and dipeptide propensities can be easily applied to the protein function prediction problems that dipeptide composition features play an important role. Availability: The used datasets, source codes of SCM, and supplementary files are available at http://iclab.life.nctu.edu.tw/SCM/.Item type:Item, Prediction and analysis of protein solubility using a novel scoring card method with dipeptide composition(2012-12-13) ;Huang, Hui-Ling ;Charoenkwan, Phasit ;Kao, Te-Fen ;Lee, Hua-ChinChang, Fang-LinBackground: Existing methods for predicting protein solubility on overexpression in Escherichia coli advance performance by using ensemble classifiers such as two-stage support vector machine (SVM) based classifiers and a number of feature types such as physicochemical properties, amino acid and dipeptide composition, accompanied with feature selection. It is desirable to develop a simple and easily interpretable method for predicting protein solubility, compared to existing complex SVM-based methods. Results: This study proposes a novel scoring card method (SCM) by using dipeptide composition only to estimate solubility scores of sequences for predicting protein solubility. SCM calculates the propensities of 400 individual dipeptides to be soluble using statistic discrimination between soluble and insoluble proteins of a training data set. Consequently, the propensity scores of all dipeptides are further optimized using an intelligent genetic algorithm. The solubility score of a sequence is determined by the weighted sum of all propensity scores and dipeptide composition. To evaluate SCM by performance comparisons, four data sets with different sizes and variation degrees of experimental conditions were used. The results show that the simple method SCM with interpretable propensities of dipeptides has promising performance, compared with existing SVM-based ensemble methods with a number of feature types. Furthermore, the propensities of dipeptides and solubility scores of sequences can provide insights to protein solubility. For example, the analysis of dipeptide scores shows high propensity of a-helix structure and thermophilic proteins to be soluble. Conclusions: The propensities of individual dipeptides to be soluble are varied for proteins under altered experimental conditions. For accurately predicting protein solubility using SCM, it is better to customize the score card of dipeptide propensities by using a training data set under the same specified experimental conditions. The proposed method SCM with solubility scores and dipeptide propensities can be easily applied to the protein function prediction problems that dipeptide composition features play an important role. Availability: The used datasets, source codes of SCM, and supplementary files are available at http://iclab.life.nctu.edu.tw/SCM/.Item type:Item, Prediction of Mouse Senescence from HE-Stain Liver Images Using an Ensemble SVM Classifier(2013) ;Huang, Hui-Ling ;Hsu, Ming-Hsin ;Lee, Hua-Chin ;Charoenkwan, PhasitHo, Shinn-JangStudy of cellular senescence from images in molecular level plays an important role in understanding the molecular basis of ageing. It is desirable to know the morphological variation between young and senescent cells. This study proposes an ensemble support vector machine (SVM) based classifier with a novel set of image features to predict mouse senescence from HE-stain liver images categorized into four classes. For the across-subject prediction that all images of the same mouse are divided into training and test images, the test accuracy is as high as 97.01% by selecting an optimal set of informative image features using an intelligent genetic algorithm. For the leave-one-subject-out prediction that the test mouse is not involved in the training images of 20 mice, we identified eight informative feature sets and established eight SVM classifiers with a single feature set. The best accuracy of using an SVM classifier is 71.73% and the ensemble classifier consisting of these eight SVM classifiers can advance performance with accuracy of 80.95%. The best two feature sets are the gray level correlation matrix for describing texture and Haralick texture set, which are good morphological features in studying cellular senescence.Item type:Item, Prediction of Non-classical Secreted Proteins Using Informative Physicochemical Properties(2010-09-01) ;Hung, Chiung-Hui ;Huang, Hui-Ling ;Hsu, Kai-Ti ;Ho, Shinn-JangHo, Shinn-YingThe prediction of non-classical secreted proteins is a significant problem for drug discovery and development of disease diagnosis. The characteristic of non-classical secreted proteins is they are leaderless proteins without signal peptides in N-terminal. This characteristic makes the prediction of non-classical proteins more difficult and complicated than the classical secreted proteins. We identify a set of informative physicochemical properties of amino acid indices cooperated with support vector machine (SVM) to find discrimination between secreted and non-secreted proteins and to predict non-classical secreted proteins. When the sequence identity of dataset was reduced to 25%, the prediction accuracy on training dataset is 85% which is much better than the traditional sequence similarity-based BLAST or PSI-BLAST tool. The accuracy of independent test is 82%. The most effective features of prediction revealed the fundamental differences of physicochemical properties between secreted and non-secreted proteins. The interpretable and valuable information could be beneficial for drug discovery or the development of new blood biochemical examinations.