Jeeva: Enterprise Grid-enabled Web Portal for Protein Secondary Structure Prediction

This paper presents a Grid portal for protein secondary structure prediction developed by using services of Aneka, a .NET-based enterprise Grid technology. The portal is used by research scientists to discover new prediction structures in a parallel manner. An SVM (Support Vector Machine)-based prediction algorithm is used with 64 sample protein sequences as a case study to demonstrate the potential of enterprise Grids.Comment: 7 page

Protein Secondary Structure Prediction Using RT-RICO: A Rule-Based Approach

Protein structure prediction has always been an important research area in biochemistry. In particular, the prediction of protein secondary structure has been a well-studied research topic. The experimental methods currently used to determine protein structure are accurate, yet costly both in terms of equipment and time. Despite the recent breakthrough of combining multiple sequence alignment information and artificial intelligence algorithms to predict protein secondary structure, the Q3 accuracy of various computational prediction methods rarely has exceeded 75%. In this paper, a newly developed rule-based data-mining approach called RT-RICO (Relaxed Threshold Rule Induction from Coverings) is presented. This method identifies dependencies between amino acids in a protein sequence and generates rules that can be used to predict secondary structure. RT-RICO achieved a Q3 score of 81.75% on the standard test dataset RS 126 and a Q3 score of 79.19% on the standard test dataset CB396, an improvement over comparable computational methods

Protein secondary structure prediction for a single-sequence using hidden semi-Markov models

BACKGROUND: The accuracy of protein secondary structure prediction has been improving steadily towards the 88% estimated theoretical limit. There are two types of prediction algorithms: Single-sequence prediction algorithms imply that information about other (homologous) proteins is not available, while algorithms of the second type imply that information about homologous proteins is available, and use it intensively. The single-sequence algorithms could make an important contribution to studies of proteins with no detected homologs, however the accuracy of protein secondary structure prediction from a single-sequence is not as high as when the additional evolutionary information is present. RESULTS: In this paper, we further refine and extend the hidden semi-Markov model (HSMM) initially considered in the BSPSS algorithm. We introduce an improved residue dependency model by considering the patterns of statistically significant amino acid correlation at structural segment borders. We also derive models that specialize on different sections of the dependency structure and incorporate them into HSMM. In addition, we implement an iterative training method to refine estimates of HSMM parameters. The three-state-per-residue accuracy and other accuracy measures of the new method, IPSSP, are shown to be comparable or better than ones for BSPSS as well as for PSIPRED, tested under the single-sequence condition. CONCLUSIONS: We have shown that new dependency models and training methods bring further improvements to single-sequence protein secondary structure prediction. The results are obtained under cross-validation conditions using a dataset with no pair of sequences having significant sequence similarity. As new sequences are added to the database it is possible to augment the dependency structure and obtain even higher accuracy. Current and future advances should contribute to the improvement of function prediction for orphan proteins inscrutable to current similarity search methods

Protein secondary structure prediction using BLAST and relaxed threshold rule induction from coverings

Protein structure prediction has always been an important research area in bioinformatics and biochemistry. Despite the recent breakthrough of combining multiple sequence alignment information and artificial intelligence algorithms to predict protein secondary structure, the Q₃ accuracy of various computational prediction methods rarely has exceeded 75%; this status has changed little since 2003 when Rost stated that the currently best methods reach a level around 77% three-state per-residue accuracy. The application of artificial neural network methods to this problem is revolutionary in the sense that those techniques employ the homologues of proteins for training and prediction. In this dissertation, a different approach, RT-RICO (Relaxed Threshold Rule Induction from Coverings), is presented that instead uses association rule mining. This approach still makes use of the fundamental principle that structure is more conserved than sequence. However, rules between each known secondary structure element and its neighboring amino acid residues are established to perform the predictions. This dissertation consists of five research articles that discuss different prediction techniques and detailed rule-generation algorithms. The most recent prediction approach, BLAST-RT-RICO, achieved a Q₃ accuracy score of 89.93% on the standard test dataset RS126 and a Q₃ score of 87.71% on the standard test dataset CB396, an improvement over comparable computational methods. Herein one research article also discusses the results of examining those RT-RICO rules using an existing association rule visualization tool, modified to account for the non-Boolean characterization of protein secondary structure --Abstract, page iv