Ontology highlight
ABSTRACT:
SUBMITTER: Scholtmeijer K
PROVIDER: S-EPMC123772 | biostudies-literature | 2002 Mar
REPOSITORIES: biostudies-literature
Scholtmeijer Karin K Janssen Meike I MI Gerssen Bertus B de Vocht Marcel L ML van Leeuwen Babs M BM van Kooten Theo G TG Wösten Han A B HA Wessels Joseph G H JG
Applied and environmental microbiology 20020301 3
Hydrophobins are small (ca. 100 amino acids) secreted fungal proteins that are characterized by the presence of eight conserved cysteine residues and by a typical hydropathy pattern. Class I hydrophobins self-assemble at hydrophilic-hydrophobic interfaces into highly insoluble amphipathic membranes, thereby changing the nature of surfaces. Hydrophobic surfaces become hydrophilic, while hydrophilic surfaces become hydrophobic. To see whether surface properties of assembled hydrophobins can be cha ...[more]