The <i>‘</i>Shape-Shifter<i>’</i> Peptide from the Disulphide Isomerase PmScsC Shows Context-Dependent Conformational Preferences

The <i>‘</i>Shape-Shifter<i>’</i> Peptide from the Disulphide Isomerase PmScsC Shows Context-Dependent Conformational Preferences

Multiple crystal structures of the homo-trimeric protein disulphide isomerase PmScsC reveal that the peptide which links the trimerization stalk and catalytic domain can adopt helical, β-strand and loop conformations. This region has been called a <i>‘</i>shape-shifter<i>’</i>...

Full description

Bibliographic Details
Main Authors: Lorna J. Smith, Chloe W. Green, Christina Redfield
Format: Article
Language:English
Published: MDPI AG 2021-04-01
Series:Biomolecules
Subjects:
NMR spectroscopy
MD simulation
X-ray crystallography
protein dynamics
chameleon sequence
protein folding
Online Access:https://www.mdpi.com/2218-273X/11/5/642

Similar Items

Similar Items