Theoretical Study of the Influence of K20N Glycosylation on the Dynamic Behavior of Im7 Protein.

ABSTRACT: This study employed molecular dynamics simulations to investigate the impact of N-linked glycosylation (GlcNAc₂) at the K20N position on the structural dynamics and stability of the bacterial immunity protein Im7. Simulations were conducted in both aqueous and 2 M urea denaturing environments. The simulation results in aqueous solution indicate that glycosylation has only a minor effect on the protein, consistent with expectations. In contrast, simulations in urea reveal that K20N glycosylation significantly destabilizes Im7. Analyses of RMSD, native contacts, SASA, RMSF, correlation matrix, PCA, helical content and hydrophobic centroid distance consistently demonstrate that K20N glycosylation increases the flexibility of Helix I and Helix II and weakens the concerted motion amo

SUBMITTER: Wang J 

PROVIDER: S-EPMC12525938 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature