解析蛋白质结对折叠的影响
Untangling the Influence of a Protein Knot on Folding.
作者信息
Capraro Dominique T, Jennings Patricia A
机构信息
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California.
Department of Chemistry and Biochemistry, University of California, San Diego, La Jolla, California.
出版信息
Biophys J. 2016 Mar 8;110(5):1044-51. doi: 10.1016/j.bpj.2016.01.017.
Entanglement and knots occur across all aspects of the physical world. Despite the common belief that knots are too complicated for incorporation into proteins, knots have been identified in the native fold of a growing number of proteins. The discovery of proteins with this unique backbone characteristic has challenged the preconceptions about the complexity of biological structures, as well as current folding theories. Given the intricacies of the knotted geometry, the interplay between a protein's fold, structure, and function is of particular interest. Interestingly, for most of these proteins, the knotted region appears critical both in folding and function, although full understanding of these contributions is still incomplete. Here, we experimentally reveal the impact of the knot on the landscape, the origin of the bistable nature of the knotted protein, and broaden the view of knot formation as uniquely decoupled from folding.
纠缠和纽结存在于物理世界的各个方面。尽管人们普遍认为纽结过于复杂，无法纳入蛋白质结构中，但越来越多的蛋白质天然折叠结构中已发现了纽结。具有这种独特主链特征的蛋白质的发现，挑战了人们对生物结构复杂性的先入之见，以及当前的折叠理论。鉴于纽结几何结构的复杂性，蛋白质折叠、结构和功能之间的相互作用尤其令人感兴趣。有趣的是，对于大多数这类蛋白质而言，纽结区域在折叠和功能方面似乎都至关重要，尽管对这些作用的全面理解仍不完整。在此，我们通过实验揭示了纽结对景观的影响、纽结蛋白双稳态性质的起源，并拓宽了纽结形成与折叠独特解耦的观点。
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