AlphaFold 3 accurately models natural variants of Helicobacter pylori catalase KatA.

ABSTRACT: Subtle changes in protein sequence can equate to large changes in function, such as enabling pathogens to evade the immune system, hindering antibody recognition of antigens, or conferring antibiotic resistance. Even single amino acid substitutions may alter ligand binding affinity, enzymatic activity, and protein stability. Yet, due to limitations in time and resources, proteins closely related in sequence to those already characterized often remain unexamined. AlphaFold has emerged as a promising tool for protein structure prediction, though its utility in modeling single amino acid substitutions remains uncertain. In this study, we assessed AlphaFold 3's accuracy in modeling natural variants of the Helicobacter pylori catalase KatA by comparing its predictions to a novel high-res

SUBMITTER: Baylink A 

PROVIDER: S-EPMC12157475 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature