We study a single statistical amphiphilic copolymer chain AB in a sele
ctive solvent (e.g. water). Two situations are considered. In the anne
aled case, hydrophilic (A) and hydrophobic (B) monomers are at local c
hemical equilibrium and both the fraction of A monomers and their loca
tion along the chain can vary, whereas in the quenched case (which is
relevant to proteins), the chemical sequence along the chain is fixed
by synthesis. In both cases, the physical behaviour depends on the ave
rage hydrophobicity of the polymer chain. For a strongly hydrophobic c
hain (large fraction of B), we find an ordinary continuous theta colla
pse, with a large conformational entropy in the collapsed phase. For a
weakly hydrophobic, or a hydrophilic chain, there is an unusual first
-order collapse transition. In particular, for the case of Gaussian di
sorder, this discontinuous transition is driven by a change of sign of
the third virial coefficient. The entropy of this collapsed phase is
strongly reduced with respect to the theta collapsed phase.