Structural elucidation of four fungal hydrophobins belonging to classes I and II: Results from Alphafold and accelerated molecular dynamics simulations.

ABSTRACT: Hydrophobins (HFB) find application in various industries including biotechnology and medical devices; therefore, it is imperative to elucidate and learn more about their folded structures. Few fungal HFB protein structures are available in the Protein Data Bank (PDB), and fewer have been elucidated using homology modeling or short molecular dynamics (MD) simulations in the literature. Moreover, many homology modeling algorithms will only model the region with sequence identity. Therefore, we turned towards the state-of-the-art, artificial intelligence powered AlphaFold. It performed well in predicting the core β-barrel, a characteristic of HFBs, except for HFB9A which was unfolded with low confidence scores. These initial structures were then prepared for accelerated MD simulation in the

SUBMITTER: Agwora D 

PROVIDER: S-EPMC11957597 | biostudies-literature | 2025

REPOSITORIES: biostudies-literature