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Force measurements of the disruption of the nascent polypeptide chain from the ribosome by optical tweezers
Author(s) -
Katranidis Alexandros,
Grange Wilfried,
Schlesinger Ramona,
Choli-Papadopoulou Theodora,
Brüggemann Dorothea,
Hegner Martin,
Büldt Georg
Publication year - 2011
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.04.045
Subject(s) - ribosome , optical tweezers , folding (dsp implementation) , polypeptide chain , chemistry , biophysics , chain (unit) , population , translation (biology) , protein folding , nanotechnology , biochemistry , physics , biology , rna , materials science , messenger rna , optics , engineering , demography , electrical engineering , amino acid , astronomy , sociology , gene
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.