RT Journal Article
SR Electronic
T1 The protein folding rate and the geometry and topology of the native state
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 2021.10.06.463425
DO 10.1101/2021.10.06.463425
A1 Jason Wang
A1 Eleni Panagiotou
YR 2021
UL http://biorxiv.org/content/early/2021/10/07/2021.10.06.463425.abstract
AB Proteins fold in 3-dimensional conformations which are important for their function. Characterizing the global conformation of proteins rigorously and separating secondary structure effects from topological effects is a challenge. New developments in Applied Knot Theory allow to characterize the topological characteristics of proteins (knotted or not). By analyzing a small set of two-state and multi-state proteins with no knots or slipknots, our results show that 95.4% of the analyzed proteins have non-trivial topological characteristics, as reflected by the second Vassiliev measure, and that the logarithm of the experimental protein folding rate depends on both the local geometry and the topology of the protein’s native state.Competing Interest StatementThe authors have declared no competing interest.