Journal
CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 60, Issue -, Pages 131-141Publisher
CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2020.01.007
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Funding
- EMBO Installation Grant [2057]
- Polish Ministry for Science and Higher Education [0003/ID3/2016/64]
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Around 6% of protein structures deposited in the PDB are entangled, forming knots, slipknots, lassos, links, and u-curves. In each of these cases, the protein backbone weaves through itself in a complex way, and at some point passes through a closed loop, formed by other regions of the protein structure. Such a passing can be interpreted as crossing a topological barrier. How proteins overcome such barriers, and therefore different degrees of frustration, challenged scientists and has shed new light on the field of protein folding. In this review, we summarize the current knowledge about the free energy landscape of proteins with non-trivial topology. We describe identified mechanisms which lead proteins to self-tying. We discuss the influence of excluded volume, such as crowding and chaperones, on tying, based on available data. We briefly discuss the diversity of topological complexity of proteins and their evolution. We also list available tools to investigate non-trivial topology. Finally, we formulate intriguing and challenging questions at the boundary of biophysics, bioinformatics, biology, and mathematics, which arise from the discovery of entangled proteins.
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