Dataset Information

FoldRec-C2C: protein fold recognition by combining cluster-to-cluster model and protein similarity network.

ABSTRACT: As a key for studying the protein structures, protein fold recognition is playing an important role in predicting the protein structures associated with COVID-19 and other important structures. However, the existing computational predictors only focus on the protein pairwise similarity or the similarity between two groups of proteins from 2-folds. However, the homology relationship among proteins is in a hierarchical structure. The global protein similarity network will contribute to the performance improvement. In this study, we proposed a predictor called FoldRec-C2C to globally incorporate the interactions among proteins into the prediction. For the FoldRec-C2C predictor, protein fold recognition problem is treated as an information retrieval task in nature language processing. The initial ranking results were generated by a surprised ranking algorithm Learning to Rank, and then three re-ranking algorithms were performed on the ranking lists to adjust the results globally based on the protein similarity network, including seq-to-seq model, seq-to-cluster model and cluster-to-cluster model (C2C). When tested on a widely used and rigorous benchmark dataset LINDAHL dataset, FoldRec-C2C outperforms other 34 state-of-the-art methods in this field. The source code and data of FoldRec-C2C can be downloaded from http://bliulab.net/FoldRec-C2C/download.

SUBMITTER: Shao J

PROVIDER: S-EPMC7454262 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature

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FoldRec-C2C: protein fold recognition by combining cluster-to-cluster model and protein similarity network.

Shao Jiangyi J Yan Ke K Liu Bin B

Briefings in bioinformatics 20210501 3

As a key for studying the protein structures, protein fold recognition is playing an important role in predicting the protein structures associated with COVID-19 and other important structures. However, the existing computational predictors only focus on the protein pairwise similarity or the similarity between two groups of proteins from 2-folds. However, the homology relationship among proteins is in a hierarchical structure. The global protein similarity network will contribute to the perform ...[more]

PMID: 32685972

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Project description:Protein fold recognition is a critical step toward protein structure and function prediction, aiming at providing the most likely fold type of the query protein. In recent years, the development of deep learning (DL) technique has led to massive advances in this important field, and accordingly, the sensitivity of protein fold recognition has been dramatically improved. Most DL-based methods take an intermediate bottleneck layer as the feature representation of proteins with new fold types. However, this strategy is indirect, inefficient and conditional on the hypothesis that the bottleneck layer's representation is assumed as a good representation of proteins with new fold types. To address the above problem, in this work, we develop a new computational framework by combining triplet network and ensemble DL. We first train a DL-based model, termed FoldNet, which employs triplet loss to train the deep convolutional network. FoldNet directly optimizes the protein fold embedding itself, making the proteins with the same fold types be closer to each other than those with different fold types in the new protein embedding space. Subsequently, using the trained FoldNet, we implement a new residue-residue contact-assisted predictor, termed FoldTR, which improves protein fold recognition. Furthermore, we propose a new ensemble DL method, termed FSD_XGBoost, which combines protein fold embedding with the other two discriminative fold-specific features extracted by two DL-based methods SSAfold and DeepFR. The Top 1 sensitivity of FSD_XGBoost increases to 74.8% at the fold level, which is ~9% higher than that of the state-of-the-art method. Together, the results suggest that fold-specific features extracted by different DL methods complement with each other, and their combination can further improve fold recognition at the fold level. The implemented web server of FoldTR and benchmark datasets are publicly available at http://csbio.njust.edu.cn/bioinf/foldtr/.

Project description:BACKGROUND: Machine learning-based methods have been proven to be powerful in developing new fold recognition tools. In our previous work [Zhang, Kochhar and Grigorov (2005) Protein Science, 14: 431-444], a machine learning-based method called DescFold was established by using Support Vector Machines (SVMs) to combine the following four descriptors: a profile-sequence-alignment-based descriptor using Psi-blast e-values and bit scores, a sequence-profile-alignment-based descriptor using Rps-blast e-values and bit scores, a descriptor based on secondary structure element alignment (SSEA), and a descriptor based on the occurrence of PROSITE functional motifs. In this work, we focus on the improvement of DescFold by incorporating more powerful descriptors and setting up a user-friendly web server. RESULTS: In seeking more powerful descriptors, the profile-profile alignment score generated from the COMPASS algorithm was first considered as a new descriptor (i.e., PPA). When considering a profile-profile alignment between two proteins in the context of fold recognition, one protein is regarded as a template (i.e., its 3D structure is known). Instead of a sequence profile derived from a Psi-blast search, a structure-seeded profile for the template protein was generated by searching its structural neighbors with the assistance of the TM-align structural alignment algorithm. Moreover, the COMPASS algorithm was used again to derive a profile-structural-profile-alignment-based descriptor (i.e., PSPA). We trained and tested the new DescFold in a total of 1,835 highly diverse proteins extracted from the SCOP 1.73 version. When the PPA and PSPA descriptors were introduced, the new DescFold boosts the performance of fold recognition substantially. Using the SCOP_1.73_40% dataset as the fold library, the DescFold web server based on the trained SVM models was further constructed. To provide a large-scale test for the new DescFold, a stringent test set of 1,866 proteins were selected from the SCOP 1.75 version. At a less than 5% false positive rate control, the new DescFold is able to correctly recognize structural homologs at the fold level for nearly 46% test proteins. Additionally, we also benchmarked the DescFold method against several well-established fold recognition algorithms through the LiveBench targets and Lindahl dataset. CONCLUSIONS: The new DescFold method was intensively benchmarked to have very competitive performance compared with some well-established fold recognition methods, suggesting that it can serve as a useful tool to assist in template-based protein structure prediction. The DescFold server is freely accessible at http://202.112.170.199/DescFold/index.html.

Dataset Information

FoldRec-C2C: protein fold recognition by combining cluster-to-cluster model and protein similarity network.

Publications

FoldRec-C2C: protein fold recognition by combining cluster-to-cluster model and protein similarity network.

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