ArticleScientific reports2017
An in-silico glimpse into the pH dependent structural changes of T7 RNA polymerase: a protein with simplicity.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 21 citations in OpenAlex.
- Molecular Basis of pH-Dependent Activity in T7 RNA Polymerase Revealed by Constant pH Replica Exchange Molecular Dynamics.ACS physical chemistry Au · 2026Article
- Efficient production of a self-amplifying RNA vaccine sequence with the single subunit RNA polymerase fromRNA (New York, N.Y.) · 2026Article
- Decoding pH-dependent structural dynamics of CHIKV nsP2 protease: insights from computational antiviral targeting.Molecular diversity · 2026Article
- Comprehensive evaluation of T7 promoter for enhanced yield and quality in mRNA production.Scientific reports · 2024Article
- Maximizing mRNA vaccine production with Bayesian optimization.Biotechnology and bioengineering · 2022Article
- Demystifying the pH dependent conformational changes of human heparanase pertaining to structure-function relationships: an in silico approach.Journal of computer-aided molecular design · 2018Article
- Critical test of isotropic periodic sum techniques with group-based cut-off schemes.Scientific reports · 2018Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The capability of performing an array of functions with its single subunit structure makes T7 RNA polymerase (T7RNAP) as one of the simplest yet attractive target for various investigations ranging from structure determinations to several biological tests. In this study, with the help of molecular dynamics (MD) calculations and molecular docking, we investigated the effect of varying pH conditions on conformational flexibility of T7RNAP. We also studied its effect on the interactions with a well established inhibitor (heparin), substrate GTP and T7 promoter of T7RNAP. The simulation studies were validated with the help of three dimensional reconstructions of the polymerase at different pH environments using transmission electron microscopy and single particle analysis. On comparing the simulated structures, it was observed that the structure of T7RNAP changes considerably and interactions with its binding partners also changes as the pH shifts from basic to acidic. Further, it was observed that the C-terminal end plays a vital role in the inefficiency of the polymerase at low pH. Thus, this in-silico study may provide a significant insight into the structural investigations on T7RNAP as well as in designing potent inhibitors against it in varying pH environments.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.