Structural characterization of the thermal unfolding pathway of human VEGFR1 D2 domain

• DOI: 10.1111/febs.16246
• Publication Date: 2021-10-24T12:53:55Z
• Authors: Donatella Diana; Rossella Di Stasi; Sara García‐Viñuales; Lucia De Rosa; Carla Isernia; Gaetano Malgieri; Danilo Milardi; Luca D. D’Andrea; Roberto Fattorusso
• Keywords: Characterization

Folding stability is a crucial feature of protein evolution and essential for functions. Thus, the comprehension folding mechanisms represents an important complement to structure function, determine structural basis misfolding. In this context, thermal unfolding studies represent useful tool get molecular description conformational transitions governing folding/unfolding equilibrium given protein. Here, we report pathway VEGFR1D2, member immunoglobulin superfamily by means high-resolution thermodynamic approach that combines differential scanning calorimetry with atomic-level monitored NMR. We show how VEGFR1D2 driven oxidatively induced disulfide pairing: key event in achievement its functional formation small hydrophobic core surrounds bridge. Such 'folding nucleus' induces cooperative transition properly folded conformation supporting hypothesis bond can act as nucleus eases process.