title: Force measurements of the disruption of the nascent polypeptide chain from the ribosome by optical tweezers.
abstract: We show that optical tweezers are a valuable tool to study the co-translational folding of a nascent polypeptide chain at the ribosome in real-time. The aim of this study was to demonstrate that a stable and intact population of ribosomes can be tethered to polystyrene beads and that specific hook-ups to the nascent polypeptide chain by dsDNA handles, immobilized on a second bead, can be detected. A rupture force of the nascent chain in the range of 10-50 pN was measured, which demonstrates that the system is anchored to the surface in a stable and specific way. This will allow in numerous future applications to follow protein folding using much lower forces.
authors.affiliation: Research Centre Jülich, Institute of Complex Systems (ICS-5), Jülich, Germany. a.katranidis@fz-juelich.de
authors.forename: Alexandros
authors.initials: A
authors.lastname: Katranidis
authors.forename: Wilfried
authors.initials: W
authors.lastname: Grange
authors.forename: Ramona
authors.initials: R
authors.lastname: Schlesinger
authors.forename: Theodora
authors.initials: T
authors.lastname: Choli-Papadopoulou
authors.forename: Dorothea
authors.initials: D
authors.lastname: Brüggemann
authors.forename: Martin
authors.initials: M
authors.lastname: Hegner
authors.forename: Georg
authors.initials: G
authors.lastname: Büldt
mesh_terms: D052898:Optical Tweezers; D010455:Peptides / Q000378:metabolism; D014176:Protein Biosynthesis; D017510:Protein Folding; D012270:Ribosomes / Q000378:metabolism
chemical_list: D010455:Peptides