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We study the medium effects on the selection of sequences in protein foldingby taking account of the surface potential in HP-model. Our analysis on theproportion of H and P monomers in the sequences gives a direct interpretationthat the lowly designable structures possess small average gap. The numericalcalculation by means of our model exhibits that the surface potential enhancesthe average gap of highly designable structures. It also shows that a moststable structure may be no longer the most stable one if the medium parameterschanged.Comment: 4 pages, 4 figure

Medium effects on the selection of sequences folding into stable proteins in a simple model