Single-molecule force spectroscopy shows that side chain interactions govern the mechanochemical response of polypeptide α‑helices and prevent the formation of β-sheets
[en] Secondary α-helix and β-sheet structures are key scaffolds around which the rest of the residues condense during protein folding. Despite their key role in numerous processes to maintain life, little...
Disciplines :
Physical, chemical, mathematical & earth Sciences: Multidisciplinary, general & others
Author, co-author :
Asano, Marie ; Université de Liège - ULiège > Département de chimie (sciences) > Nanochimie et systèmes moléculaires
Sluysmans, Damien ; Université de Liège - ULiège > Département de chimie (sciences) ; Université de Liège - ULiège > Molecular Systems (MolSys)
Willet, Nicolas ; Université de Liège - ULiège > Département de chimie (sciences) > Nanochimie et systèmes moléculaires
Bonduelle, Colin
Lecommandoux, Sébastien
Duwez, Anne-Sophie ; Université de Liège - ULiège > Département de chimie (sciences) > Nanochimie et systèmes moléculaires
Language :
English
Title :
Single-molecule force spectroscopy shows that side chain interactions govern the mechanochemical response of polypeptide α‑helices and prevent the formation of β-sheets
