Backbone and sidechain ¹H, ¹³C and ¹⁵N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans

Vanessa K Morris; Ann H Kwan; Joel P Mackay; Margaret Sunde

doi:10.1007/s12104-011-9330-5

Backbone and sidechain ¹H, ¹³C and ¹⁵N chemical shift assignments of the hydrophobin DewA from Aspergillus nidulans

Biomol NMR Assign. 2012 Apr;6(1):83-6. doi: 10.1007/s12104-011-9330-5. Epub 2011 Aug 4.

Authors

Vanessa K Morris¹, Ann H Kwan, Joel P Mackay, Margaret Sunde

Affiliation

¹ School of Molecular Bioscience, Building G08, University of Sydney, Sydney, NSW 2006, Australia.

PMID: 21845363
DOI: 10.1007/s12104-011-9330-5

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.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Amino Acid Sequence
Aspergillus nidulans*
Fungal Proteins / chemistry*
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular*
Protein Structure, Secondary

Substances

DEWA protein, Asperigillus nidulans
Fungal Proteins