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FAH paper listed amongst best of 2012 by Biophysical Journal

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<p><a class="asset-img-link" href="http://onlinedigeditions.com/publication/frame.php?i=144258&p=&pn=&ver=flex" style="float: right;" target="_self"><img alt="BiophysJ-bestof2012-cover" border="0" class="asset asset-image at-xid-6a00e54ef157d78834017d4162de4e970c" src="http://folding.typepad.com/.a/6a00e54ef157d78834017d4162de4e970c-800wi" style="margin: 0px 0px 5px 5px;" title="BiophysJ-bestof2012-cover" /></a>Biophysical Journal announced their "<a href="http://onlinedigeditions.com/publication/frame.php?i=144258&p=&pn=&ver=flex" target="_self">Best of 2012</a>" paper collection. We were excited that <a href="http://www.ncbi.nlm.nih.gov/pubmed/22385857" target="_self">one of our papers was included</a>. That work, "Protein Folding is Mechanistically Robust" investigates how key aspects of FAH technology (MSMs) can yield new insights into protein folding in some unexpected ways. Congratulations to Jeffery Weber for his work. We've posted the technical abstract below as well.</p>

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<p><strong>ABSTRACT. </strong>Markov state models (MSMs) have proven to be useful tools in simulating large and slowly-relaxing biological systems like proteins. MSMs model proteins through dynamics on a discrete-state energy landscape, allowing molecules to effectively sample large regions of phase space. In this work, we use aspects of MSMs to ask: is protein folding mechanistically robust? We first provide a definition of mechanism in the context of Markovian models, and we later use perturbation theory and the concept of parametric sloppiness to show that parts of the MSM eigenspectrum are resistant to perturbation. We introduce a new, to our knowledge, Bayesian metric by which eigenspectrum robustness can be evaluated, and we discuss the implications of mechanistic robustness and possible new applications of MSMs to understanding biophysical phenomena.</p>

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