scholarly journals Protein Secondary Structure Detection in Intermediate-Resolution Cryo-EM Maps using Deep Learning

2020 ◽  
Vol 118 (3) ◽  
pp. 43a
Author(s):  
Sai Raghavendra Maddhuri Venkata Subramaniya ◽  
Genki Terashi ◽  
Daisuke Kihara
2019 ◽  
Vol 16 (9) ◽  
pp. 911-917 ◽  
Author(s):  
Sai Raghavendra Maddhuri Venkata Subramaniya ◽  
Genki Terashi ◽  
Daisuke Kihara

Optik ◽  
2020 ◽  
Vol 216 ◽  
pp. 164703
Author(s):  
Kai Tong ◽  
Yunxuan Wang ◽  
Fucheng Wang ◽  
Jiaru Sun ◽  
Xiaogang Wu

2019 ◽  
Author(s):  
Aminur Rab Ratul ◽  
Marcel Turcotte ◽  
M. Hamed Mozaffari ◽  
WonSook Lee

AbstractProtein secondary structure is crucial to create an information bridge between the primary structure and the tertiary (3D) structure. Precise prediction of 8-state protein secondary structure (PSS) significantly utilized in the structural and functional analysis of proteins in bioinformatics. In this recent period, deep learning techniques have been applied in this research area and raise the Q8 accuracy remarkably. Nevertheless, from a theoretical standpoint, there still lots of room for improvement, specifically in 8-state (Q8) protein secondary structure prediction. In this paper, we presented two deep learning architecture, namely 1D-Inception and BD-LSTM, to improve the performance of 8-classes PSS prediction. The input of these two architectures is a carefully constructed feature matrix from the sequence features and profile features of the proteins. Firstly, 1D-Inception is a Deep convolutional neural network-based approach that was inspired by the InceptionV3 model and containing three inception modules. Secondly, BD-LSTM is a recurrent neural network model which including bidirectional LSTM layers. Our proposed 1D-Inception method achieved 76.65%, 71.18%, 76.86%, and 74.07% Q8 accuracy respectively on benchmark CullPdb6133, CB513, CASP10, and CASP11 datasets. Moreover, BD-LSTM acquired 74.71%, 69.49%, 74.07%, and 72.37% state-8 accuracy after evaluated on CullPdb6133, CB513, CASP10, and CASP11 datasets, respectively. Both these architectures enable the efficient processing of local and global interdependencies between amino acids to make an accurate prediction of each class is very beneficial in the deep neural network. To the best of our knowledge, experiment results of the 1D-Inception model demonstrate that it outperformed all the state-of-art methods on the benchmark CullPdb6133, CB513, and CASP10 datasets.


2019 ◽  
Author(s):  
◽  
Jie Hou

Protein structure prediction is one of the most important scientific problems in the field of bioinformatics and computational biology. The availability of protein three-dimensional (3D) structure is crucial for studying biological and cellular functions of proteins. The importance of four major sub-problems in protein structure prediction have been clearly recognized. Those include, first, protein secondary structure prediction, second, protein fold recognition, third, protein quality assessment, and fourth, multi-domain assembly. In recent years, deep learning techniques have proved to be a highly effective machine learning method, which has brought revolutionary advances in computer vision, speech recognition and bioinformatics. In this dissertation, five contributions are described. First, DNSS2, a method for protein secondary structure prediction using one-dimensional deep convolution network. Second, DeepSF, a method of applying deep convolutional network to classify protein sequence into one of thousands known folds. Third, CNNQA and DeepRank, two deep neural network approaches to systematically evaluate the quality of predicted protein structures and select the most accurate model as the final protein structure prediction. Fourth, MULTICOM, a protein structure prediction system empowered by deep learning and protein contact prediction. Finally, SAXSDOM, a data-assisted method for protein domain assembly using small-angle X-ray scattering data. All the methods are available as software tools or web servers which are freely available to the scientific community.


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