Next Talks

  • Date: March 8, 2019
  • Speaker: Sophie E. Jackson

Title: Why are there knots in proteins?


There are now more than 1700 protein chains that are known to contain some type of topological knot in their polypeptide chains in the protein structure databank. Although this number is small relative to the total number of protein structures solved, it is remarkably high given the fact that for decades it was thought impossible for a protein chain to fold and thread in such a way as to create a knotted structure. There are four different types of knotted protein structures that contain 31, 41, 52 and 61 knots and over the past 15 years there has been an increasing number of experimental and computational studies on these systems. The folding pathways of knotted proteins have been studied in some detail, however, the focus of this talk is to address the fundamental question “Why are there knots in proteins?” It is known that once formed, knotted protein structures tend to be conserved by nature. This, in addition to the fact that, at least for some deeply knotted proteins, their folding rates are slow compared with many unknotted proteins, has led to the hypothesis that there are some properties of knotted proteins that are different from unknotted ones, and that this had resulted in some evolutionary advantage over faster folding unknotted structures. In this talk, I will review the evidence for and against this theory. In particular, how a knot within a protein chain may affect the thermodynamic, kinetic, mechanical and cellular (resistance to degradation) stability of the protein will be discussed.


protein structure, protein stability, knotted proteins, methyltransferase, ubiquitin c-terminal hydrolase, knot-promoting loops, UCH-L1, YibK, YbeA

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