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T Charles Hodgman

Publications and source records attributed to T Charles Hodgman.

3 recordsLinked to original sources

A bio-basis function neural network for protein peptide cleavage activity characterisation.

This paper presents a novel neural learning algorithm for analysing protein peptides which comprise amino acids as non-numerical attributes. The algorithm is derived from the radial basis function neural networks (RBFNNs) and is referred to as a bio-basis function neural network (BBFNN). The basic principle is to replace the radial basis function used by RBFNNs with a bio-basis function. Each basis in BBFNN is supported by a peptide. The bases collectively form a feature space, in which each basis represents a feature dimension. A linear classifier is constructed in the feature space for characterising a protein peptide in terms of functional status. The theoretical basis of BBFNN is that peptides, which perform the same function will have similar compositions of amino acids. Because of this, the similarity between peptides can have statistical significance for modelling while the proposed bio-basis function can well code this information from data. The application to two real cases shows that BBFNN outperformed multi-layer perceptrons and support vector machines.

Algorithms↗

Characterizing proteolytic cleavage site activity using bio-basis function neural networks.

MOTIVATION: In protein chemistry, proteomics and biopharmaceutical development, there is a desire to know not only where a protein is cleaved by a protease, but also the susceptibility of its cleavage sites. The current tools for proteolytic cleavage prediction have often relied purely on regular expressions, or involve models that do not represent biological data well. RESULTS: A novel methodology for characterizing proteolytic cleavage site activities has been developed, which incorporates two fundamental features: activity class prediction and the use of an amino acid similarity matrix for (non-parametric) neural learning. The first solved the problem of predicting proteolytic efficiency. The second significantly improved the robustness in prediction and reduced the time complexity for learning. This study shows that activity class prediction is successful when applying this methodology to the prediction and characterization of Trypsin cleavage sites and the prediction of HIV protease cleavage sites. AVAILABILITY: Requests for software and data should be made respectively to Dr Zheng Rong Yang and Miss Rebecca Thomson.

Amino Acid Sequence↗

Searching for discrimination rules in protease proteolytic cleavage activity using genetic programming with a min-max scoring function.

This paper presents an algorithm which is able to extract discriminant rules from oligopeptides for protease proteolytic cleavage activity prediction. The algorithm is developed using genetic programming. Three important components in the algorithm are a min-max scoring function, the reverse Polish notation (RPN) and the use of minimum description length. The min-max scoring function is developed using amino acid similarity matrices for measuring the similarity between an oligopeptide and a rule, which is a complex algebraic equation of amino acids rather than a simple pattern sequence. The Fisher ratio is then calculated on the scoring values using the class label associated with the oligopeptides. The discriminant ability of each rule can therefore be evaluated. The use of RPN makes the evolutionary operations simpler and therefore reduces the computational cost. To prevent overfitting, the concept of minimum description length is used to penalize over-complicated rules. A fitness function is therefore composed of the Fisher ratio and the use of minimum description length for an efficient evolutionary process. In the application to four protease datasets (Trypsin, Factor Xa, Hepatitis C Virus and HIV protease cleavage site prediction), our algorithm is superior to C5, a conventional method for deriving decision trees.

Algorithms↗