Abstract
Understanding how natural proteins fold spontaneously onto their specific, biologically functional 3D structures is both a fascinating fundamental problem in modern biochemistry and a necessary step toward developing technologies for protein engineering and designing protein-based nanodevices. One of the limitations that scientists working in this area have encountered in the past, however, has been the difficulty in connecting analytical theory to experimental results. For a long time experimentalists could not use theory to interpret their results. Theoretical predictions, moreover, were not amenable to experimental testing. Such limitations have been progressively eliminated by the combination of key theoretical concepts, improved simulations, and new experiments and their detailed quantitative analysis with simple statistical mechanical models. The work of Inanami et al. in PNAS (1) provides a remarkable example of how powerful these simple theoretical models can be in explaining the complexities and nuances of protein folding reactions.
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