STUDY OF PROTEIN FOLDING USING THE LATTICE MODEL WITH UNRESTRICTED BOUNDARY.

xProtein folding in a two-dimensional lattice with an unrestricted boundary is simulated by means of the simplified HP model. The proteins are regarded as peptide chains and fold into compact structures. These structures are classified by the number of core sites. It is found that the number of structures with the given designability and given number of core sites versus designability appears as the normal distribution. The simulation shows that the structures with a large number of core sites have a high designability. [ABSTRACT FROM AUTHOR]