Hysteresis as a Marker for Complex, Overlapping Landscapes in Proteins

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• 作者：Benjamin T. Andrews ; Dominique T. Capraro ; Joanna I. Sulkowska ; Jos茅 N. Onuchic ; Patricia A. Jennings
• 刊名：The Journal of Physical Chemistry Letters
• 出版年：2013
• 出版时间：January 3, 2013
• 年：2013
• 卷：4
• 期：1
• 页码：180-188
• 全文大小：404K
• 年卷期：v.4,no.1(January 3, 2013)
• ISSN：1948-7185

文摘

Topologically complex proteins fold by multiple routes as a result of hard-to-fold regions of the proteins. Oftentimes, these regions are introduced into the protein scaffold for function and increase frustration in the otherwise smooth-funneled landscape. Interestingly, while functional regions add complexity to folding landscapes, they may also contribute to a unique behavior referred to as hysteresis. While hysteresis is predicted to be rare, it is observed in various proteins, including proteins containing a unique peptide cyclization to form a fluorescent chromophore as well as proteins containing a knotted topology in their native fold. Here, hysteresis is demonstrated to be a consequence of the decoupling of unfolding events from the isomerization or hula-twist of a chromophore in one protein and the untying of the knot in a second protein system. The question now is can hysteresis be a marker for the interplay of landscapes where complex folding and functional regions overlap?