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the claim
Optimal window size significantly impacts protein secondary structure prediction accuracy.
the verdict
CONTESTED
contested - the weight sits with the supporting side
refutedsupported
the weight of evidence
2 sources for · 0 against

The literature notes that protein secondary structure prediction is challenging and numerous approaches have been proposed to improve accuracy, but the provided sources do not specifically establish that optimal window size significantly impacts accuracy.

Evidence for · 2
2023 · cited by 15
Protein secondary structure prediction (PSSP) is a challenging task in computational biology. However, existing models with deep architectures are not sufficient and comprehensive for deep long-range feature extraction of long sequences. This paper proposes a novel deep learning model to improve Protein secondary structure prediction. In the model, our proposed bidirectional temporal convolutional network (BTCN) can extract the bidirectional deep local dependencies in protein sequences segmented by the sliding window technique, the bidirectional long short-term memory (BLSTM) network can extract the global interactions between residues, and our proposed multi-scale bidirectional temporal convolutional network (MSBTCN) can further capture the bidirectional multi-scale long-range features of residues while preserving the hidden layer information more comprehensively. In particular, we also propose that fusing the features of 3-state and 8-state Protein secondary structure prediction can further improve the prediction accuracy. Moreover, we also propose and compare multiple novel deep models by combining bidirectional long short-term memory with temporal convolutional network (TCN), reverse temporal convolutional network (RTCN), multi-scale temporal convolutional network (multi-scale bidirectional temporal convolutional network), bidirectional temporal convolutional network and multi-scale bidirectional temporal convolutional network, respectively. Furthermore, we demonstrate that the reverse prediction of secondary structure outperforms the forward prediction, suggesting that amino acids at later positions have a greater impact on secondary structure recognition. Experimental results on benchmark datasets including CASP10, CASP11, CASP12, CASP13, CASP14, and CB513 show that our methods achieve better prediction performance compared to five state-of-the-art methods.
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The analysis

rails:sufficiency:supported:single_source:for=1+1p:against=0+0p | v55:sufficiency | v55:coherence_repaired:what=both

More for · 1
2025 · cited by 4
Protein Secondary Structure Prediction (PSSP) is regarded as a challenging task in bioinformatics, and numerous approaches to achieve a more accurate prediction have been proposed. Accurate PSSP can be instrumental in inferring protein tertiary structure and their functions. Machine Learning and in particular Deep Learning approaches show promising results for the PSSP problem. In this paper, we deploy a Convolutional Neural Network (CNN) trained with the Subsampled Hessian Newton (SHN) method (a Hessian Free Optimisation variant), with a two- dimensional input representation of embeddings extracted from a language model pretrained with protein sequences. Utilising a CNN trained with the SHN method and the input embeddings, we achieved on average a 79.96% per residue (Q3) accuracy on the CB513 dataset and 81.45% Q3 accuracy on the PISCES dataset (without any post-processing techniques applied). The application of ensembles and filtering techniques to the results of the CNN improved the overall prediction performance. The Q3 accuracy on the CB513 increased to 93.65% and for the PISCES dataset to 87.13%. Moreover, our method was evaluated using the CASP13 dataset where we showed that as the post-processing window size increased, the prediction performance increased as well. In fact, with the biggest post-processing window size (limited by the smallest CASP13 protein), we achieved a Q3 accuracy of 98.12% and a Segment Overlap (SOV) score of 96.98 on the CASP13 dataset when the CNNs were trained with the PISCES dataset. Finally, we showed that input representations from embeddings can perform equally well as representations extracted from multiple sequence alignments.
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  1. Ensemble deep learning models for protein secondary structure prediction using bidirectional temporal convolution and bidirectional long short-term memorypeer-reviewedno side taken
  2. Post-processing enhances protein secondary structure prediction with second order deep learning and embeddingspeer-reviewedno side taken
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