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A Statistical Similarity/Dissimilarity Analysis of Protein Sequences Based on a Novel Group Representative Vector.

ABSTRACT: Similarity/dissimilarity analysis is a key way of understanding the biology of an organism by knowing the origin of the new genes/sequences. Sequence data are grouped in terms of biological relationships. The number of sequences related to any group is susceptible to be increased every day. All the present alignment-free methods approve the utility of their approaches by producing a similarity/dissimilarity matrix. Although this matrix is clear, it measures the degree of similarity among sequences individually. In our work, a representative of each of three groups of protein sequences is introduced. A similarity/dissimilarity vector is evaluated instead of the ordinary similarity/dissimilarity matrix based on the group representative. The approach is applied on three selected groups of protein sequences: beta globin, NADH dehydrogenase subunit 5 (ND5), and spike protein sequences. A cross-grouping comparison is produced to ensure the singularity of each group. A qualitative comparison between our approach, previous articles, and the phylogenetic tree of these protein sequences proved the utility of our approach.

SUBMITTER: Abd Elwahaab MA

PROVIDER: S-EPMC6530227 | biostudies-literature | 2019

REPOSITORIES: biostudies-literature

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A Statistical Similarity/Dissimilarity Analysis of Protein Sequences Based on a Novel Group Representative Vector.

Abd Elwahaab Marwa A MA Abo-Elkhier Mervat M MM Abo El Maaty Moheb I MI

BioMed research international 20190508

Similarity/dissimilarity analysis is a key way of understanding the biology of an organism by knowing the origin of the new genes/sequences. Sequence data are grouped in terms of biological relationships. The number of sequences related to any group is susceptible to be increased every day. All the present alignment-free methods approve the utility of their approaches by producing a similarity/dissimilarity matrix. Although this matrix is clear, it measures the degree of similarity among sequenc ...[more]

PMID: 31205946

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Project description:This paper introduces "Kabirian-based optinalysis (KBO)," a pioneering framework that addresses the longstanding challenges in estimating symmetry/asymmetry, similarity/dissimilarity, and identity/unidentity within mathematical structures and biological sequences. The existing methods often lack a strong theoretical foundation, leading to inconsistencies and limitations. Kabirian-based optinalysis draws inspiration from isomorphism and automorphism, providing a theoretically grounded framework that unifies estimation methodologies. It introduces the concept of optiscale, autoreflective pairing, isoreflective pairing, and others ensuring invariance and robustness under various mathematical transformations and establishing functional bijectivity for isomorphic or automorphic structures. This not only overcomes previous limitations but also offers precise and interpretable estimations. Additionally, the framework introduces "geometrical pairwise analysis" to improve sensitivity to position-specific and character-specific variations in biological sequences. This novel approach enhances the accuracy of sequence similarity assessments, surpassing the constraints of conventional methods. The novelty of this work extends beyond mathematics and biology, impacting diverse fields such as computer science, data analysis, pattern recognition, and evolutionary biology. Kabirian-based optinalysis presents a holistic and theoretically grounded solution that has the potential to revolutionize the analysis of complex structures and sequences, opening new horizons for interdisciplinary research.•Inspired by automorphism and isomorphism, Kabirian-based optinalysis introduces a new paradigm-shifting and unified approach to estimations in mathematical structures and biological sequences with a solid conceptual and theoretical foundation.•The GPA method enhances pairwise sequence similarity estimation by being sensitive to position-specific and character-specific variations and providing a comprehensive characterization of these features.

Project description:BACKGROUND: The rapid burgeoning of available protein data makes the use of clustering within families of proteins increasingly important. The challenge is to identify subfamilies of evolutionarily related sequences. This identification reveals phylogenetic relationships, which provide prior knowledge to help researchers understand biological phenomena. A good evolutionary model is essential to achieve a clustering that reflects the biological reality, and an accurate estimate of protein sequence similarity is crucial to the building of such a model. Most existing algorithms estimate this similarity using techniques that are not necessarily biologically plausible, especially for hard-to-align sequences such as proteins with different domain structures, which cause many difficulties for the alignment-dependent algorithms. In this paper, we propose a novel similarity measure based on matching amino acid subsequences. This measure, named SMS for Substitution Matching Similarity, is especially designed for application to non-aligned protein sequences. It allows us to develop a new alignment-free algorithm, named CLUSS, for clustering protein families. To the best of our knowledge, this is the first alignment-free algorithm for clustering protein sequences. Unlike other clustering algorithms, CLUSS is effective on both alignable and non-alignable protein families. In the rest of the paper, we use the term "phylogenetic" in the sense of "relatedness of biological functions". RESULTS: To show the effectiveness of CLUSS, we performed an extensive clustering on COG database. To demonstrate its ability to deal with hard-to-align sequences, we tested it on the GH2 family. In addition, we carried out experimental comparisons of CLUSS with a variety of mainstream algorithms. These comparisons were made on hard-to-align and easy-to-align protein sequences. The results of these experiments show the superiority of CLUSS in yielding clusters of proteins with similar functional activity. CONCLUSION: We have developed an effective method and tool for clustering protein sequences to meet the needs of biologists in terms of phylogenetic analysis and prediction of biological functions. Compared to existing clustering methods, CLUSS more accurately highlights the functional characteristics of the clustered families. It provides biologists with a new and plausible instrument for the analysis of protein sequences, especially those that cause problems for the alignment-dependent algorithms.

Project description:BackgroundPredicting protein function from primary sequence is an important open problem in modern biology. Not only are there many thousands of proteins of unknown function, current approaches for predicting function must be improved upon. One problem in particular is overly-specific function predictions which we address here with a new statistical model of the relationship between protein sequence similarity and protein function similarity.MethodologyOur statistical model is based on sets of proteins with experimentally validated functions and numeric measures of function specificity and function similarity derived from the Gene Ontology. The model predicts the similarity of function between two proteins given their amino acid sequence similarity measured by statistics from the BLAST sequence alignment algorithm. A novel aspect of our model is that it predicts the degree of function similarity shared between two proteins over a continuous range of sequence similarity, facilitating prediction of function with an appropriate level of specificity.SignificanceOur model shows nearly exact function similarity for proteins with high sequence similarity (bit score >244.7, e-value >1e(-62), non-redundant NCBI protein database (NRDB)) and only small likelihood of specific function match for proteins with low sequence similarity (bit score <54.6, e-value <1e(-05), NRDB). For sequence similarity ranges in between our annotation model shows an increasing relationship between function similarity and sequence similarity, but with considerable variability. We applied the model to a large set of proteins of unknown function, and predicted functions for thousands of these proteins ranging from general to very specific. We also applied the model to a data set of proteins with previously assigned, specific functions that were electronically based. We show that, on average, these prior function predictions are more specific (quite possibly overly-specific) compared to predictions from our model that is based on proteins with experimentally determined function.

Dataset Information

A Statistical Similarity/Dissimilarity Analysis of Protein Sequences Based on a Novel Group Representative Vector.

Publications

A Statistical Similarity/Dissimilarity Analysis of Protein Sequences Based on a Novel Group Representative Vector.

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