Structural analysis of hydrophobins.
Hydrophobins are a remarkable class of small cysteine-rich proteins found exclusively in fungi. They self-assemble to form robust polymeric monolayers that are highly amphipathic and play numerous roles in fungal biology, such as in the formation and dispersal of aerial spores and in pathogenic and mutualistic interactions. The polymeric form can be reversibly disassembled and is able to reverse the wettability of a surface, leading to many proposals for nanotechnological applications over recent years. The surprising properties of hydrophobins and their potential for commercialization have led to substantial efforts to delineate their morphology and molecular structure. In this review, we summarize the progress that has been made using a variety of spectroscopic and microscopic approaches towards understanding the molecular mechanisms underlying hydrophobin structure.
Sunde
Margaret
M
School of Molecular and Microbial Biosciences, University of Sydney, Sydney 2006, Australia.
Kwan
Ann H Y
AH
Templeton
Matthew D
MD
Beever
Ross E
RE
Mackay
Joel P
JP
D005656:Fungal Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism / Q000502:physiology*; D005658:Fungi / Q000737:chemistry / Q000254:growth & development / Q000378:metabolism / Q000502:physiology*; D011487:Protein Conformation
D005656:Fungal Proteins