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* Department of Chemical Engineering, North Carolina State University, Raleigh, North Carolina 27695-7905; and Department of Physiology and Biophysics, State University of New York at Buffalo, Buffalo, New York 14214
Correspondence: Address reprint requests to Carol K. Hall, E-mail: hall{at}turbo.che.ncsu.edu.
We have performed discontinuous molecular dynamic simulations of the assembly and folding kinetics of a tetrameric ß-sheet complex that contains four identical four-stranded antiparallel ß-sheet peptides. The potential used in the simulation is a hybrid Go-type potential characterized by the bias gap parameter g, an artificial measure of a model protein's preference for its native state, and the intermolecular contact parameter 
, which measures the ratio of intermolecular to intramolecular native attractions. The formation of the ß-sheet complex and its equilibrium properties strongly depend on the size of the intermolecular contact parameter . The ordered ß-sheet complex in the folded state and nonaligned ß-sheets or tangled chains in the misfolded state are distinguished by measuring the squared radius of gyration 
and the fraction of native contacts Q. The folding yield for the folded state is high at intermediate values of , but is low at both small and large values of . The folded state at small is liquid-like, but is solid-like at both intermediate and large . The misfolded state at small contains nonaligned ß-sheets and tangled chains with poor secondary structure at large . Various folding pathways via dimeric and trimeric intermediates are observed, depending on . Comparison with experimental results on protein aggregation indicates that intermediate values are most appropriate for modeling fibril formation and small values are most appropriate for modeling the formation of amorphous aggregates.
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