Computational Engineering of the MS2 Lysis Protein to Modulate Lysis Timing and Improve Viral Yield (Mini-documentation) Abstract Bacteriophage lysis timing plays a critical role in virion assembly efficiency and viral yield. In the MS2 bacteriophage system, the small membrane-associated L protein is responsible for host lysis and may be influenced by structural alterations caused by amino acid substitutions. This mini computational study evaluated previously reported MS2 L-protein mutations associated with altered lysis phenotypes to determine whether these variants preserved structurally plausible membrane-associated conformations. Mutant variants (L44P, F47Y, and R30L) were computationally generated from the WT MS2 L-protein sequence and analyzed using Benchling Boltz-2 and AlphaFold2 structural prediction approaches. Comparative structural analysis revealed that all variants preserved alpha-helical membrane-associated regions to varying degrees, although mutations produced distinct local conformational perturbations. Among the evaluated candidates, R30L displayed the closest structural similarity to the WT prediction, whereas L44P showed stronger local structural alterations consistent with the helix-disrupting properties of proline residues. These results suggest that selected MS2-L mutations may preserve structural plausibility while potentially altering local structural dynamics relevant to lysis-associated behavior. This work provides a preliminary computational framework for future experimental phage-engineering studies focused on lysis timing modulation and viral yield optimization.