Mechanical unfolding of a knotted protein unveils the kinetic and thermodynamic consequences of threading a polypeptide chain.

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 Rep

journal_title

Scientific reports

authors

Rivera M,Hao Y,Maillard RA,Baez M

doi

10.1038/s41598-020-66258-5

subject

Has Abstract

pub_date

2020-06-12 00:00:00

pages

9562

issue

1

issn

2045-2322

pii

10.1038/s41598-020-66258-5

journal_volume

10

pub_type

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