PROTEIN-FOLDING BY A BIASED MONTE-CARLO PROCEDURE IN THE DIHEDRAL ANGLE SPACE

A straightforward method for predicting the protein structure is to fi nd conformations that have the lowest energy along a chosen folding pa thway, One approach in this direction is to produce a large number of structures by varying the dihedral angles of the molecule more or less randomly and then to screen each one using a suitable energy function , This procedure is computationally demanding, but by using a more rea listic model, one hopes that the folding behavior one observes in calc ulations may better mimic the actual folding process in nature, The me thod is beginning to yield interesting results, thanks to the increase in the computational power but also to the intelligent selection of t he folding pathway, This article reviews general features of this meth od, some important highlights of the particular procedure we used, and some of the more significant results obtained to date in our laborato ry, The results are highly encouraging and indicate the direction of f uture effort that is most likely to be fruitful.