Ontology highlight
ABSTRACT:
SUBMITTER: Bustamante A
PROVIDER: S-EPMC5691195 | biostudies-literature | 2017 Nov
REPOSITORIES: biostudies-literature
Bustamante Andrés A Sotelo-Campos Juan J Guerra Daniel G DG Floor Martin M Wilson Christian A M CAM Bustamante Carlos C Báez Mauricio M
Nature communications 20171117 1
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<sup>-1</sup>. Monte Carlo dynamics of random chains predict this value, indicating ...[more]