ArticleJournal of animal science and technology2015
In silico characterisation, homology modelling and structure-based functional annotation of blunt snout bream (Megalobrama amblycephala) Hsp70 and Hsc70 proteins.
Article in Journal of animal science and technology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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10 citing papers in PubMed.
- Comparative genomic and evolutionary analysis of the heat shock protein gene family in the chicken genome.Animal biotechnology · 2026Article
- An in silico approach for screening non-synonymous SNPs in Mycobacterium tuberculosis PPE68 protein and impact on structure.Scientific reports · 2025Article
- Identification and Characterization of theGenes · 2025Article
- Exploration of Canarium odontophyllum fruit phytoconstituents as potential candidates against epilepsy using in silico studies.Journal, genetic engineering & biotechnology · 2025Article
- Article
- An In Silico Design of Peptides Targeting the S1/S2 Cleavage Site of the SARS-CoV-2 Spike Protein.Viruses · 2023Article
- In Silico Design of a Chimeric Humanized L-asparaginase.International journal of molecular sciences · 2023Article
- Plant catalase in silico characterization and phylogenetic analysis with structural modeling.Journal, genetic engineering & biotechnology · 2022Article
- Insights from the protein sequence and structure analysis of PgHsc70 and OsHsp70 genes.Bioinformation · 2022Article
- Levofloxacin is phytotoxic and modifies the protein profile of lupin seedlings.Environmental science and pollution research international · 2017Article
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3 authors.
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Abstract
backgroundHeat shock proteins play an important role in protection from stress stimuli and metabolic insults in almost all organisms.
methodsIn this study, computational tools were used to deeply analyse the physicochemical characteristics and, using homology modelling, reliably predict the tertiary structure of the blunt snout bream (Ma-) Hsp70 and Hsc70 proteins. Derived three-dimensional models were then used to predict the function of the proteins.
resultsPreviously published predictions regarding the protein length, molecular weight, theoretical isoelectric point and total number of positive and negative residues were corroborated. Among the new findings are: the extinction coefficient (33725/33350 and 35090/34840 - Ma-Hsp70/ Ma-Hsc70, respectively), instability index (33.68/35.56 - both stable), aliphatic index (83.44/80.23 - both very stable), half-life estimates (both relatively stable), grand average of hydropathicity (-0.431/-0.473 - both hydrophilic) and amino acid composition (alanine-lysine-glycine/glycine-lysine-aspartic acid were the most abundant, no disulphide bonds, the N-terminal of both proteins was methionine). Homology modelling was performed by SWISS-MODEL program and the proposed model was evaluated as highly reliable based on PROCHECK's Ramachandran plot, ERRAT, PROVE, Verify 3D, ProQ and ProSA analyses.
conclusionsThe research revealed a high structural similarity to Hsp70 and Hsc70 proteins from several taxonomically distant animal species, corroborating a remarkably high level of evolutionary conservation among the members of this protein family. Functional annotation based on structural similarity provides a reliable additional indirect evidence for a high level of functional conservation of these two genes/proteins in blunt snout bream, but it is not sensitive enough to functionally distinguish the two isoforms.
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