P. Sneha

TL;DR: High-end computational methods, such as molecular dynamics (MD) simulation has proved to be a constitutive approach to detecting the minor changes associated with an SNP for better understanding of the structural and functional relationship.

TL;DR: A systematic search was implemented using four literature databases to capture all the causative mutations of Glucose-6-phosphate dehydrogenase (G6PD) deficiency in the 22 Arab countries, yielding 33 mutations that were exposed to structural analysis and molecular dynamics simulation analysis.

TL;DR: The deleterious mutant V54M was mapped, modeled the mutant protein complex, and deciphered the impact of mutation on binding with its partner telethonin in the titin crystal structure of PDB ID: 1YA5 with the aid of docking analysis to understand the mechanistic action of V 54M mutation in altering the protein structure, dynamics, and stability.

TL;DR: This study suggests that the four mutations might affect thePRPS1 protein function and stability of the structure, and may serve as a platform for drug repositioning and personalized medicine for diseases that are caused by the PRPS1 deficiency.

TL;DR: The HNF1A protein was retrieved from public databases and subjected to a three-step computational mutational analysis to identify the underlying mechanism and the MD approach is an important tool for elucidating the impact and affinity of mutations in DNA-protein interactions and understanding their function.