%0 Journal Article %J Science %D 1990 %T Simulations of the folding of a globular protein %A Jeffrey Skolnick %A Andrzej Koliński %X Dynamic Monte Carlo simulations of the folding of a globular protein, apoplastocyanin, have been undertaken in the context of a new lattice model of proteins that includes both side chains and a-carbon backbone atoms and that can approximate native conformations at the level of 2 angstroms (root mean square) or better. Starting from random-coil unfolded states, the model apoplastocyanin was folded to a native conformation that is topologically similar to the real protein. The present simulations used a marginal propensity for local secondary structure consistent with but by no means enforcing the native conformation and a full hydrophobicity scale in which any nonbonded pair of side chains could interact. These molecules folded through a punctuated on-site mechanism of assembly where folding initiated at or near one of the turns ultimately found in the native conformation. Thus these simulations represent a partial solution to the globular-protein folding problem. %B Science %V 250 %P 1121–1125 %G eng %U http://cssb.biology.gatech.edu/skolnick/publications/pdffiles/087.pdf %R 10.1126/science.250.4984.1121