title: Backbone and sidechain ¹H, ¹³C and ¹⁵N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans.
abstract: Hydrophobins are proteins secreted by filamentous fungi that are able to self-assemble into monolayers at hydrophobic:hydrophilic interfaces. The layers are amphipathic and can reverse the wettability of surfaces. Hydrophobins have several roles in fungal development, including the formation of coatings on fungal structures to render them hydrophobic. Here we report the backbone and sidechain assignments for the class I hydrophobin DewA from the fungus Aspergillus nidulans.
authors.affiliation: School of Molecular Bioscience, Building G08, University of Sydney, Sydney, NSW 2006, Australia.
authors.forename: Vanessa K
authors.initials: VK
authors.lastname: Morris
authors.forename: Ann H
authors.initials: AH
authors.lastname: Kwan
authors.forename: Joel P
authors.initials: JP
authors.lastname: Mackay
authors.forename: Margaret
authors.initials: M
authors.lastname: Sunde
mesh_terms: D000595:Amino Acid Sequence; D001233:Aspergillus nidulans; D005656:Fungal Proteins / Q000737:chemistry*; D008969:Molecular Sequence Data; D019906:Nuclear Magnetic Resonance, Biomolecular; D017433:Protein Structure, Secondary
chemical_list: C095254:DEWA protein, Asperigillus nidulans; D005656:Fungal Proteins