In silico induction of missense mutation in NNRTI protein: computational modelling and stability study of modelled proteins.

The paper presents in silico mutational research on the energetics of the most resolved protein structure of HIV-1 NNRTIs, the 4G1Q HIV-1 reverse transcriptase protein. Twenty nearby residues that are less than 6 Å from the center of the embedded ligand are subjected to in silico alterations. For the current study, 380 unique proteins are generated in silico using a set of 380 surrounding residues that have been altered. Analyses and comparison with the parent protein have been done to determine the impact of mutation on the change in folding-unfolding free energy (G), protein stability, and solvation energy. To evaluate the impact of mutation (i) by and (ii) on a particular amino acid residue, a two-fold investigation is conducted. The findings imply that in 12 designed proteins (G − 3.0), folding-unfolding is significantly favored, resulting in the creation of a highly stable conformation. The 11 designed proteins are unstable because the positive values of G > 0.5 in these proteins point to unfavorable mutations. However, the G value in 171 designed proteins is − 1.0, which suggests that mutations cause designed proteins to adopt a stable conformation. According to the findings, out of the 380 created proteins, 11 had extremely unfavorable, 69 less-favorable, and 270 favorable folding-unfolding changes. [ABSTRACT FROM AUTHOR]