Quantifying biomolecular hydrophobicity: Single molecule force spectroscopy of class II hydrophobins.

ABSTRACT: Hydrophobins are surface-active proteins produced by filamentous fungi. The amphiphilic structure of hydrophobins is very compact, containing a distinct hydrophobic patch on one side of the molecule, locked by four intramolecular disulfide bridges. Hydrophobins form dimers and multimers in solution to shield these hydrophobic patches from water exposure. Multimer formation in solution is dynamic, and hydrophobin monomers can be exchanged between multimers. Unlike class I hydrophobins, class II hydrophobins assemble into highly ordered films at the air-water interface. In order to increase our understanding of the strength and nature of the interaction between hydrophobins, we used atomic force microscopy for single molecule force spectroscopy to explore the molecular interaction forces bet

SUBMITTER: Paananen A 

PROVIDER: S-EPMC8164047 | biostudies-literature | 2021 Jan-Jun

REPOSITORIES: biostudies-literature