cnnAlpha : Protein disordered regions prediction by reduced amino acid alphabets and convolutional neural networks

2020 ◽  
Vol 88 (11) ◽  
pp. 1472-1481
Author(s):  
Mauricio Oberti ◽  
Iosif I. Vaisman
PeerJ ◽  
2018 ◽  
Vol 6 ◽  
pp. e4750 ◽  
Author(s):  
Afshine Amidi ◽  
Shervine Amidi ◽  
Dimitrios Vlachakis ◽  
Vasileios Megalooikonomou ◽  
Nikos Paragios ◽  
...  

During the past decade, with the significant progress of computational power as well as ever-rising data availability, deep learning techniques became increasingly popular due to their excellent performance on computer vision problems. The size of the Protein Data Bank (PDB) has increased more than 15-fold since 1999, which enabled the expansion of models that aim at predicting enzymatic function via their amino acid composition. Amino acid sequence, however, is less conserved in nature than protein structure and therefore considered a less reliable predictor of protein function. This paper presents EnzyNet, a novel 3D convolutional neural networks classifier that predicts the Enzyme Commission number of enzymes based only on their voxel-based spatial structure. The spatial distribution of biochemical properties was also examined as complementary information. The two-layer architecture was investigated on a large dataset of 63,558 enzymes from the PDB and achieved an accuracy of 78.4% by exploiting only the binary representation of the protein shape. Code and datasets are available at https://github.com/shervinea/enzynet.


2021 ◽  
Author(s):  
Anastasiya V Kulikova ◽  
Daniel J Diaz ◽  
James M Loy ◽  
Andrew D Ellington ◽  
Claus O Wilke

The fundamental problem of protein biochemistry is to predict protein structure from amino acid sequence. The inverse problem, predicting either entire sequences or individual mutations that are consistent with a given protein structure, has received much less attention even though it has important applications in both protein engineering and evolutionary biology. Here, we ask whether 3D convolutional neural networks (3D CNNs) can learn the local fitness landscape of protein structure to reliably predict either the wild-type amino acid or the consensus in a multiple sequence alignment from the local structural context surrounding a site of interest. We find that the network can predict wild type with good accuracy, and that network confidence is a reliable measure of whether a given prediction is likely going to be correct or not. Predictions of consensus are less accurate, and are primarily driven by whether or not the consensus matches the wild type. Our work suggests that high-confidence mis-predictions of the wild type may identify sites that are primed for mutation and likely targets for protein engineering.


2020 ◽  
Vol 2020 (10) ◽  
pp. 28-1-28-7 ◽  
Author(s):  
Kazuki Endo ◽  
Masayuki Tanaka ◽  
Masatoshi Okutomi

Classification of degraded images is very important in practice because images are usually degraded by compression, noise, blurring, etc. Nevertheless, most of the research in image classification only focuses on clean images without any degradation. Some papers have already proposed deep convolutional neural networks composed of an image restoration network and a classification network to classify degraded images. This paper proposes an alternative approach in which we use a degraded image and an additional degradation parameter for classification. The proposed classification network has two inputs which are the degraded image and the degradation parameter. The estimation network of degradation parameters is also incorporated if degradation parameters of degraded images are unknown. The experimental results showed that the proposed method outperforms a straightforward approach where the classification network is trained with degraded images only.


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