Title : Extremophiles protein structural, functional and evolutionary adaptation driven by its structural plasticity is proven by different physicochemical factors
Abstract:
Several microorganisms can live in a variety of harsh conditions, including high temperatures, low pH, and high salt concentrations. Extremophile stability is offered by ensembles of multiple weak connections, which causes compactness-rigidity in proteins, limiting their flexibility and function. Understanding how microbial proteins change structurally under stress is crucial. A vast number of protein sequences and structures were systematically studied to understand protein stability and distinguish microbial extremophilic proteins from their non-extremophilic orthologs. The results demonstrated that environmental pressures influenced the method for packing the protein core through substitutive structural processes and improved ionic interaction. According to data analysis, there is a difference in the number and composition of amino acids among them. The lack of a functional relationship between most extremophile and non-extremophile proteins in microorganisms was shown by the negative correlation of pairwise sequence alignments and structure alignments. A significant number of salt bridges were detected on the surface of the extremostable proteins. A large number of tiny nonpolar amino acids and a modest number of charged amino acids, such as Arginine and Aspartic acid, have higher nonplanar Omega angles in their peptide bonds. In severe environments, microorganisms may predispose amino acid composition, including geometric variability, to molecular adaptation of extremostable proteins to atmospheric fluctuations and related alterations under natural selection pressure. Variation in amino acid content and structural diversification in microbial proteins play a key role in evolutionary adaptation in different climatic conditions.
What will audience learn from your presentation?
- This study will aid in the improvement of enzyme stability in general, including chemical usage, protein engineering, and immobilisation.
- The biophysical pleiotropy of extremostable proteins was also used to develop a global prediction model for assuming the effect of mutations on protein stability.
- How adaptative mechanisms of extremosable proteins will help to mitigate climatic changes throughout the evolutionary time sscale.
