The amino acid sequences of the class I hydrophobins are
diverse, with long and varied intercysteine spacings (C1-8-C2C3-
38-C4-23-C5-7-C6C7-21-C8; the number marked in italics indicates
the longest stretch of amino acids between cysteine residues
observed in a class I sequence alignment; Figure 2). Class I hydrophobins
form monolayers with fibrillar substructures known as
rodlets. The rodlets are extremely robust and can only be depolymerized
by treatment with strong acids.13,14