Cytosolic Interactome Protects Against Protein Unfolding in a Single Molecule Experiment
Barbara Scalvini (Universiteit Leiden)
Laurens W.H.J. Heling (Universiteit Leiden)
Vahid Sheikhhassani (Universiteit Leiden)
Vanda Sunderlikova (AMOLF Institute for Atomic and Molecular Physics)
Sander J. Tans (AMOLF Institute for Atomic and Molecular Physics, TU Delft - BN/Sander Tans Lab)
Alireza Mashaghi (Universiteit Leiden)
More Info
expand_more
Other than for strictly personal use, it is not permitted to download, forward or distribute the text or part of it, without the consent of the author(s) and/or copyright holder(s), unless the work is under an open content license such as Creative Commons.
Abstract
Single molecule techniques are particularly well suited for investigating the processes of protein folding and chaperone assistance. However, current assays provide only a limited perspective on the various ways in which the cellular environment can influence the folding pathway of a protein. In this study, a single molecule mechanical interrogation assay is developed and used to monitor protein unfolding and refolding within a cytosolic solution. This allows to test the cumulative topological effect of the cytoplasmic interactome on the folding process. The results reveal a stabilization against forced unfolding for partial folds, which are attributed to the protective effect of the cytoplasmic environment against unfolding and aggregation. This research opens the possibility of conducting single molecule molecular folding experiments in quasi-biological environments.
help_outline