scholarly journals Bio-informed Protein Sequence Generation for Multi-class Virus Mutation Prediction

2020 ◽  
Author(s):  
Yuyang Wang ◽  
Prakarsh Yadav ◽  
Rishikesh Magar ◽  
Amir Barati Farimani
Keyword(s):  
Protein Sequence ◽  
Protein Sequences ◽  
Large Family ◽  
Viral Genomes ◽  
Sequence Generation ◽  
Antigen Epitope ◽  
Antigen Protein ◽  
Global Threat ◽  
Mutation Prediction ◽  
High Possibility

AbstractViral pandemics are emerging as a serious global threat to public health, like the recent outbreak of COVID-19. Viruses, especially those belonging to a large family of +ssRNA viruses, have a high possibility of mutating by inserting, deleting, or substituting one or multiple genome segments. It is of great importance for human health worldwide to predict the possible virus mutations, which can effectively avoid the potential second outbreak. In this work, we develop a GAN-based multi-class protein sequence generative model, named ProteinSeqGAN. Given the viral species, the generator is modeled on RNNs to predict the corresponding antigen epitope sequences synthesized by viral genomes. Additionally, a Graphical Protein Autoencoder (GProAE) built upon VAE is proposed to featurize proteins bioinformatically. GProAE, as a multi-class discriminator, also learns to evaluate the goodness of protein sequences and predict the corresponding viral species. Further experiments show that our ProteinSeqGAN model can generate valid antigen protein sequences from both bioinformatics and statistics perspectives, which can be promising predictions of virus mutations.

scholarly journals Ancestral sequences of a large promiscuous enzyme family correspond to bridges in sequence space in a network representation

2021 ◽  
Vol 18 (184) ◽  
Author(s):  
Patrick C. F. Buchholz ◽  
Bert van Loo ◽  
Bernard D. G. Eenink ◽  
Erich Bornberg-Bauer ◽  
Jürgen Pleiss
Keyword(s):  
Protein Sequence ◽  
Protein Sequences ◽  
Large Family ◽  
Time Axis ◽  
Pairwise Sequence Identity ◽  
Consensus Sequences ◽  
Sequence Identity ◽  
Ancestral Sequences ◽  
Hierarchical Grouping ◽  
Ancestral Protein

Evolutionary relationships of protein families can be characterized either by networks or by trees. Whereas trees allow for hierarchical grouping and reconstruction of the most likely ancestral sequences, networks lack a time axis but allow for thresholds of pairwise sequence identity to be chosen and, therefore, the clustering of family members with presumably more similar functions. Here, we use the large family of arylsulfatases and phosphonate monoester hydrolases to investigate similarities, strengths and weaknesses in tree and network representations. For varying thresholds of pairwise sequence identity, values of betweenness centrality and clustering coefficients were derived for nodes of the reconstructed ancestors to measure the propensity to act as a bridge in a network. Based on these properties, ancestral protein sequences emerge as bridges in protein sequence networks. Interestingly, many ancestral protein sequences appear close to extant sequences. Therefore, reconstructed ancestor sequences might also be interpreted as yet-to-be-identified homologues. The concept of ancestor reconstruction is compared to consensus sequences, too. It was found that hub sequences in a network, e.g. reconstructed ancestral sequences that are connected to many neighbouring sequences, share closer similarity with derived consensus sequences. Therefore, some reconstructed ancestor sequences can also be interpreted as consensus sequences.

scholarly journals Protein Sequence Classification with Improved Extreme Learning Machine Algorithms

2014 ◽  
Vol 2014 ◽  
pp. 1-12 ◽  
Author(s):  
Jiuwen Cao ◽  
Lianglin Xiong
Keyword(s):  
Extreme Learning Machine ◽  
Protein Sequence ◽  
Protein Sequences ◽  
Activation Function ◽  
Majority Voting ◽  
Training Algorithms ◽  
Sequence Classification ◽  
Protein Sequence Classification ◽  
Learning Machine ◽  
Majority Voting Method

Precisely classifying a protein sequence from a large biological protein sequences database plays an important role for developing competitive pharmacological products. Comparing the unseen sequence with all the identified protein sequences and returning the category index with the highest similarity scored protein, conventional methods are usually time-consuming. Therefore, it is urgent and necessary to build an efficient protein sequence classification system. In this paper, we study the performance of protein sequence classification using SLFNs. The recent efficient extreme learning machine (ELM) and its invariants are utilized as the training algorithms. The optimal pruned ELM is first employed for protein sequence classification in this paper. To further enhance the performance, the ensemble based SLFNs structure is constructed where multiple SLFNs with the same number of hidden nodes and the same activation function are used as ensembles. For each ensemble, the same training algorithm is adopted. The final category index is derived using the majority voting method. Two approaches, namely, the basic ELM and the OP-ELM, are adopted for the ensemble based SLFNs. The performance is analyzed and compared with several existing methods using datasets obtained from the Protein Information Resource center. The experimental results show the priority of the proposed algorithms.

scholarly journals Techniques for the verification of minimal phylogenetic trees illustrated with ten mammalian haemoglobin sequences

1980 ◽  
Vol 187 (1) ◽  
pp. 65-74 ◽  
Author(s):  
D Penny ◽  
M D Hendy ◽  
L R Foulds
Keyword(s):  
Amino Acid ◽  
Phylogenetic Tree ◽  
Protein Sequence ◽  
Phylogenetic Trees ◽  
Sequence Data ◽  
Protein Sequences ◽  
Nucleotide Sequences ◽  
Amino Acid Sequences ◽  
Minimal Tree ◽  
Protein Sequence Data

We have recently reported a method to identify the shortest possible phylogenetic tree for a set of protein sequences [Foulds Hendy & Penny (1979) J. Mol. Evol. 13. 127–150; Foulds, Penny & Hendy (1979) J. Mol. Evol. 13, 151–166]. The present paper discusses issues that arise during the construction of minimal phylogenetic trees from protein-sequence data. The conversion of the data from amino acid sequences into nucleotide sequences is shown to be advantageous. A new variation of a method for constructing a minimal tree is presented. Our previous methods have involved first constructing a tree and then either proving that it is minimal or transforming it into a minimal tree. The approach presented in the present paper progressively builds up a tree, taxon by taxon. We illustrate this approach by using it to construct a minimal tree for ten mammalian haemoglobin alpha-chain sequences. Finally we define a measure of the complexity of the data and illustrate a method to derive a directed phylogenetic tree from the minimal tree.

scholarly journals Coupling Between Protein Level Selection and Codon Usage Optimization in the Evolution of Bacteria and Archaea

mBio ◽  
2014 ◽  
Vol 5 (2) ◽  
Author(s):  
Wenqi Ran ◽  
David M. Kristensen ◽  
Eugene V. Koonin
Keyword(s):  
Codon Usage ◽  
Protein Level ◽  
Codon Usage Bias ◽  
Protein Sequence ◽  
Gc Content ◽  
Protein Sequences ◽  
Microbial Evolution ◽  
Fine Tuning ◽  
Selection For ◽  
Genomic Gc Content

ABSTRACT The relationship between the selection affecting codon usage and selection on protein sequences of orthologous genes in diverse groups of bacteria and archaea was examined by using the Alignable Tight Genome Clusters database of prokaryote genomes. The codon usage bias is generally low, with 57.5% of the gene-specific optimal codon frequencies (F opt ) being below 0.55. This apparent weak selection on codon usage contrasts with the strong purifying selection on amino acid sequences, with 65.8% of the gene-specific dN/dS ratios being below 0.1. For most of the genomes compared, a limited but statistically significant negative correlation between F opt and dN/dS was observed, which is indicative of a link between selection on protein sequence and selection on codon usage. The strength of the coupling between the protein level selection and codon usage bias showed a strong positive correlation with the genomic GC content. Combined with previous observations on the selection for GC-rich codons in bacteria and archaea with GC-rich genomes, these findings suggest that selection for translational fine-tuning could be an important factor in microbial evolution that drives the evolution of genome GC content away from mutational equilibrium. This type of selection is particularly pronounced in slowly evolving, “high-status” genes. A significantly stronger link between the two aspects of selection is observed in free-living bacteria than in parasitic bacteria and in genes encoding metabolic enzymes and transporters than in informational genes. These differences might reflect the special importance of translational fine-tuning for the adaptability of gene expression to environmental changes. The results of this work establish the coupling between protein level selection and selection for translational optimization as a distinct and potentially important factor in microbial evolution. IMPORTANCE Selection affects the evolution of microbial genomes at many levels, including both the structure of proteins and the regulation of their production. Here we demonstrate the coupling between the selection on protein sequences and the optimization of codon usage in a broad range of bacteria and archaea. The strength of this coupling varies over a wide range and strongly and positively correlates with the genomic GC content. The cause(s) of the evolution of high GC content is a long-standing open question, given the universal mutational bias toward AT. We propose that optimization of codon usage could be one of the key factors that determine the evolution of GC-rich genomes. This work establishes the coupling between selection at the level of protein sequence and at the level of codon choice optimization as a distinct aspect of genome evolution.

GEMPROT: visualization of the impact on the protein of the genetic variants found on each haplotype

2018 ◽  
Vol 35 (14) ◽  
pp. 2492-2494
Author(s):  
Tania Cuppens ◽  
Thomas E Ludwig ◽  
Pascal Trouvé ◽  
Emmanuelle Genin
Keyword(s):  
Genetic Variants ◽  
Protein Sequence ◽  
Sequence Data ◽  
Protein Sequences ◽  
Supplementary Information ◽  
Analysis Tool ◽  
Functional Protein ◽  
Key Players ◽  
On Line ◽  
The Impact

Abstract Summary When analyzing sequence data, genetic variants are considered one by one, taking no account of whether or not they are found in the same individual. However, variant combinations might be key players in some diseases as variants that are neutral on their own can become deleterious when associated together. GEMPROT is a new analysis tool that allows, from a phased vcf file, to visualize the consequences of the genetic variants on the protein. At the level of an individual, the program shows the variants on each of the two protein sequences and the Pfam functional protein domains. When data on several individuals are available, GEMPROT lists the haplotypes found in the sample and can compare the haplotype distributions between different sub-groups of individuals. By offering a global visualization of the gene with the genetic variants present, GEMPROT makes it possible to better understand the impact of combinations of genetic variants on the protein sequence. Availability and implementation GEMPROT is freely available at https://github.com/TaniaCuppens/GEMPROT. An on-line version is also available at http://med-laennec.univ-brest.fr/GEMPROT/. Supplementary information Supplementary data are available at Bioinformatics online.

scholarly journals Measuring Similarity among Protein Sequences Using a New Descriptor

2019 ◽  
Vol 2019 ◽  
pp. 1-10 ◽  
Author(s):  
Mervat M. Abo-Elkhier ◽  
Marwa A. Abd Elwahaab ◽  
Moheb I. Abo El Maaty
Keyword(s):  
Protein Sequence ◽  
Nadh Dehydrogenase ◽  
Graphical Representation ◽  
Protein Sequences ◽  
Computation Time ◽  
Fundamental Aspect ◽  
Beta Globin ◽  
Nadh Dehydrogenase Subunit ◽  
The Public ◽  
Sequencing Technologies

The comparison of protein sequences according to similarity is a fundamental aspect of today’s biomedical research. With the developments of sequencing technologies, a large number of protein sequences increase exponentially in the public databases. Famous sequences’ comparison methods are alignment based. They generally give excellent results when the sequences under study are closely related and they are time consuming. Herein, a new alignment-free method is introduced. Our technique depends on a new graphical representation and descriptor. The graphical representation of protein sequence is a simple way to visualize protein sequences. The descriptor compresses the primary sequence into a single vector composed of only two values. Our approach gives good results with both short and long sequences within a little computation time. It is applied on nine beta globin, nine ND5 (NADH dehydrogenase subunit 5), and 24 spike protein sequences. Correlation and significance analyses are also introduced to compare our similarity/dissimilarity results with others’ approaches, results, and sequence homology.

scholarly journals Protein Sequence Comparison Based on Physicochemical Properties and the Position-Feature Energy Matrix

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Lulu Yu ◽  
Yusen Zhang ◽  
Ivan Gutman ◽  
Yongtang Shi ◽  
Matthias Dehmer
Keyword(s):  
Physicochemical Properties ◽  
Protein Sequence ◽  
Sequence Comparison ◽  
Protein Sequences ◽  
Local Dynamic ◽  
Order Information ◽  
Energy Matrix ◽  
Graph Energy ◽  
Feature Based ◽  
Protein Sequence Comparison

Abstract We develop a novel position-feature-based model for protein sequences by employing physicochemical properties of 20 amino acids and the measure of graph energy. The method puts the emphasis on sequence order information and describes local dynamic distributions of sequences, from which one can get a characteristic B-vector. Afterwards, we apply the relative entropy to the sequences representing B-vectors to measure their similarity/dissimilarity. The numerical results obtained in this study show that the proposed methods leads to meaningful results compared with competitors such as Clustal W.

scholarly journals Protein Sequence Comparison and DNA-binding Protein Identification with Generalized PseAAC and Graphical Representation

2018 ◽  
Vol 21 (2) ◽  
pp. 100-110 ◽  
Author(s):  
Chun Li ◽  
Jialing Zhao ◽  
Changzhong Wang ◽  
Yuhua Yao
Keyword(s):  
Dna Binding ◽  
Protein Sequence ◽  
Protein Identification ◽  
Binding Proteins ◽  
Graphical Representation ◽  
Sequence Data ◽  
Protein Sequences ◽  
Dna Binding Proteins ◽  
Support Vector ◽  
Letter Sequence

Aim and Objective: The rapid increase in the amount of protein sequence data available leads to an urgent need for novel computational algorithms to analyze and compare these sequences. This study is undertaken to develop an efficient computational approach for timely encoding protein sequences and extracting the hidden information. Methods: Based on two physicochemical properties of amino acids, a protein primary sequence was converted into a three-letter sequence, and then a graph without loops and multiple edges and its geometric line adjacency matrix were obtained. A generalized PseAAC (pseudo amino acid composition) model was thus constructed to characterize a protein sequence numerically. Results: By using the proposed mathematical descriptor of a protein sequence, similarity comparisons among β-globin proteins of 17 species and 72 spike proteins of coronaviruses were made, respectively. The resulting clusters agreed well with the established taxonomic groups. In addition, a generalized PseAAC based SVM (support vector machine) model was developed to identify DNA-binding proteins. Experiment results showed that our method performed better than DNAbinder, DNA-Prot, iDNA-Prot and enDNA-Prot by 3.29-10.44% in terms of ACC, 0.056-0.206 in terms of MCC, and 1.45-15.76% in terms of F1M. When the benchmark dataset was expanded with negative samples, the presented approach outperformed the four previous methods with improvement in the range of 2.49-19.12% in terms of ACC, 0.05-0.32 in terms of MCC, and 3.82- 33.85% in terms of F1M. Conclusion: These results suggested that the generalized PseAAC model was very efficient for comparison and analysis of protein sequences, and very competitive in identifying DNA-binding proteins.

scholarly journals Protein sequence profile prediction using ProtAlbert transformer1

2021 ◽  
Author(s):  
Fatemeh Zare-Mirakabad ◽  
Armin Behjati ◽  
Seyed Shahriar Arab ◽  
Abbas Nowzari-Dalini
Keyword(s):  
Amino Acids ◽  
Protein Sequence ◽  
Nearest Neighbor ◽  
Tertiary Structure ◽  
Query Sequence ◽  
Protein Secondary Structure ◽  
Protein Sequences ◽  
Family Characteristics ◽  
Sequence Profile ◽  
Protein Sequence Profile

Protein sequences can be viewed as a language; therefore, we benefit from using the models initially developed for natural languages such as transformers. ProtAlbert is one of the best pre-trained transformers on protein sequences, and its efficiency enables us to run the model on longer sequences with less computation power while having similar performance with the other pre-trained transformers. This paper includes two main parts: transformer analysis and profile prediction. In the first part, we propose five algorithms to assess the attention heads in different layers of ProtAlbert for five protein characteristics, nearest-neighbor interactions, type of amino acids, biochemical and biophysical properties of amino acids, protein secondary structure, and protein tertiary structure. These algorithms are performed on 55 proteins extracted from CASP13 and three case study proteins whose sequences, experimental tertiary structures, and HSSP profiles are available. This assessment shows that although the model is only pre-trained on protein sequences, attention heads in the layers of ProtAlbert are representative of some protein family characteristics. This conclusion leads to the second part of our work. We propose an algorithm called PA_SPP for protein sequence profile prediction by pre-trained ProtAlbert using masked-language modeling. PA_SPP algorithm can help the researchers to predict an HSSP profile while there are no similar sequences to a query sequence in the database for making the HSSP profile.

scholarly journals Protein Fold Prediction for Protein Sequences of Low Identity Based on Evolutionary and Spatial Features Using Random Forest Algorithm

2020 ◽  
Vol 10 (5) ◽  
pp. 6306-6316
Keyword(s):  
Random Forest ◽  
Protein Sequence ◽  
Tertiary Structure ◽  
Protein Sequences ◽  
Benchmark Dataset ◽  
Protein Fold ◽  
Random Forest Algorithm ◽  
Structural Class ◽  
Fold Prediction ◽  
Better Than

Protein fold prediction is a milestone step towards predicting protein tertiary structure from protein sequence. It is considered one of the most researched topics in the area of Computational Biology. It has applications in the area of structural biology and medicines. Extracting sensitive features for prediction is a key step in protein fold prediction. The actionable features are extracted from keywords of sequence header and secondary structure representations of protein sequence. The keywords holding species information are used as features after verifying with uniref100 dataset using TaxId. Prominent patterns are identified experimentally based on the nature of protein structural class and protein fold. Global and native features are extracted capturing the nature of patterns experimentally. It is found that keywords based features have positive correlation with protein folds. Keywords indicating species are important for observing functional differences which help in guiding the prediction process. SCOPe 2.07 and EDD datasets are used. EDD is a benchmark dataset and SCOPe 2.07 is the latest and largest dataset holding astral protein sequences. The training set of SCOPe 2.07 is trained using 93 dimensional features vector using Random forest algorithm. The prediction results of SCOPe 2.07 test set reports the accuracy of better than 95%. The accuracy achieved on benchmark dataset EDD is better than 93%, which is best reported as per our knowledge.

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