Abstract:
:Knots are remarkable topological features in nature. The presence of knots in crystallographic structures of proteins have stimulated considerable research to determine the kinetic and thermodynamic consequences of threading a polypeptide chain. By mechanically manipulating MJ0366, a small single domain protein harboring a shallow trefoil knot, we allow the protein to refold from either the knotted or the unknotted denatured state to characterize the free energy profile associated to both folding pathways. By comparing the stability of the native state with reference to the knotted and unknotted denatured state we find that knotting the polypeptide chain of MJ0366 increase the folding energy barrier in a magnitude close to the energy cost of forming a knot randomly in the denatured state. These results support that a protein knot can be formed during a single cooperative step of folding but occurs at the expenses of a large increment on the free energy barrier.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Rivera M,Hao Y,Maillard RA,Baez Mdoi
10.1038/s41598-020-66258-5subject
Has Abstractpub_date
2020-06-12 00:00:00pages
9562issue
1issn
2045-2322pii
10.1038/s41598-020-66258-5journal_volume
10pub_type
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