My review of Assassin's Creed: Brotherhood has gone up at GameCritics, but in case you don't want to bother, the summary is that Brotherhood is great and you should get it. It's not great like War and Peace is great. Brotherhood completely squanders all the awesome things you could do thematically with the horrible Papacy of Alexander VI and instead uses that as a backdrop for more of its tediously silly techno-conspiracy mumbo-jumbo. And, it's not great like Saint Peter's Basilica is great, because its poor design choices and occasionally slapdash construction deny it any real feel of majesty. Brotherhood is great like a really delicious dinner at a new restaurant with horrible decor. It's different, and fun, and you just can't understand some of the choices that were made in the setup.
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In the Monod-Wyman-Changeux model for cooperative binding, proteins exist in an equilibrium of low-affinity and high-affinity states in solution, absent any ligand. In this view, although it may appear that the binding of a ligand causes a conformational transition, it actually stabilizes one conformation from a pre-existing equilibrium. In the past several years, advanced NMR techniques have yielded increasing evidence that these structural equilibria exist for a number of proteins, suggesting that this model for linkage between conformational change and binding may be quite general. An upcoming paper in the Journal of Molecular Biology (1) is typical of such findings.
