pH-dependent structural diversity of profilin allergens determines thermal stability

• DOI: 10.3389/falgy.2022.1007000
• Publication Date: 2022-10-17T05:31:36Z
• Authors: Florian Hofer; Anna-Lena Fischer; Anna S. Kamenik; Franz Waibl; Monica L. Fernánd...; Klaus R. Liedl
• Keywords: Profilin; Dihedral angle; Thermal Stability; Residue (chemistry)

The family of profilin allergens is a common class proteins found in plants, viruses and various eukaryotes including mammals. Profilins are characterized by an evolutionary conserved structural fold, which responsible for their cross-reactive nature Immunoglobulin E (IgE) antibodies. Despite high overall similarity, they exhibit substantial differences biophysical properties, such as thermal pH stability. To understand the origin these functional Amb 8, Art v 4 Bet 2, we performed constant molecular dynamics simulation combination with Gaussian accelerated MD simulations. Depending on respective protonation at different levels, find distinct conformational flexibility, consistent experimentally determined melting temperatures. These variations flexibility accompanied ensemble shifts landscape quantified localized residue-wise B-factors dihedral entropies. findings strengthen link between Thus, our results clearly show importance considering dependent ensembles solution to elucidate structurally similar allergens.