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The energy cost of polypeptide knot formation and its folding consequences.

Abstract：

:Knots are natural topologies of chains. Yet, little is known about spontaneous knot formation in a polypeptide chain-an event that can potentially impair its folding-and about the effect of a knot on the stability and folding kinetics of a protein. Here we used optical tweezers to show that the free energy cost to form a trefoil knot in the denatured state of a polypeptide chain of 120 residues is 5.8 ± 1 kcal mol-1. Monte Carlo dynamics of random chains predict this value, indicating that the free energy cost of knot formation is of entropic origin. This cost is predicted to remain above 3 kcal mol-1 for denatured proteins as large as 900 residues. Therefore, we conclude that naturally knotted proteins cannot attain their knot randomly in the unfolded state but must pay the cost of knotting through contacts along their folding landscape.

journal_name

Nat Commun

journal_title

Nature communications

authors

Bustamante A,Sotelo-Campos J,Guerra DG,Floor M,Wilson CAM,Bustamante C,Báez M

doi

10.1038/s41467-017-01691-1

subject

Has Abstract

pub_date

2017-11-17 00:00:00

pages

1581

issue

1

issn

2041-1723

pii

10.1038/s41467-017-01691-1

journal_volume

8

pub_type

杂志文章

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