Abstract:
:Hydrophobins are fungal proteins characterised by their amphipathic properties and an idiosyncratic pattern of eight cysteine residues involved in four disulphide bridges. The soluble form of these proteins spontaneously self-assembles at hydrophobic/hydrophilic interfaces to form an amphipathic monolayer. The RodA hydrophobin of the opportunistic pathogen Aspergillus fumigatus forms an amyloid layer with a rodlet morphology that covers the surface of fungal spores. This rodlet layer bestows hydrophobicity to the spores facilitating their dispersal in the air and rendering the conidia inert relative to the human immune system. As a first step in the analysis of the solution structure and self-association of RodA, we report the (1)H, (13)C and (15)N resonance assignments of the soluble monomeric form of RodA.
journal_name
Biomol NMR Assignjournal_title
Biomolecular NMR assignmentsauthors
Pille A,Kwan AH,Cheung I,Hampsey M,Aimanianda V,Delepierre M,Latge JP,Sunde M,Guijarro JIdoi
10.1007/s12104-014-9555-1subject
Has Abstractpub_date
2015-04-01 00:00:00pages
113-8issue
1eissn
1874-2718issn
1874-270Xjournal_volume
9pub_type
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