This paper describes a simulation system that has been developed to model the deformation and fracture of solid objects in a real-time gaming context. Based around a corotational tetrahedral finite element method, this system has been constructed from components published in the graphics and computational physics literatures. The goal of this paper is to describe how these components can be combined to produce an engine that is robust to unpredictable user interactions, fast enough to model reasonable scenarios at real-time speeds, suitable for use in the design of a game level, and with appropriate controls allowing content creators to match artistic direction. Details concerning parallel implementation, solver design, rendering method, and other aspects of the simulation are elucidated with the intent of providing a guide to others wishing to implement similar systems. Examples from in-game scenes captured on the Xbox 360, PS3, and PC platforms are included. © 2009 ACM.

Modern life is essentially homochiral, containing D-sugars in nucleic acid backbones and L-amino acids in proteins. Since coded proteins are theorized to have developed from a prebiotic RNA World, the homochirality of L-amino acids observed in all known life presumably resulted from chiral transfer from a homochiral D-RNA World. This transfer would have been mediated by aminoacyl-RNAs defining the genetic code. Previous work on aminoacyl transfer using tRNA mimics has suggested that aminoacylation using D-RNA may be inherently biased toward reactivity with L-amino acids, implying a deterministic path from a D-RNA World to L-proteins. Using a model system of self-aminoacylating D-ribozymes and epimerizable activated amino acid analogs, we test the chiral selectivity of 15 ribozymes derived from an exhaustive search of sequence space. All of the ribozymes exhibit detectable selectivity, and a substantial fraction react preferentially to produce the D-enantiomer of the product. Furthermore, chiral preference is conserved within sequence families. These results are consistent with the transfer of chiral information from RNA to proteins but do not support an intrinsic bias of D-RNA for L-amino acids. Different aminoacylation structures result in different directions of chiral selectivity, such that L-proteins need not emerge from a D-RNA World.