Open access raw data under the CC BY licence.

Publication name: 
Chaperones Skp and SurA dynamically expand unfolded OmpX and synergistically disassemble oligomeric aggregates

Authors:
Neharika Chamachi 1,§, Andreas Hartmann 1,§, Mai Quynh Ma 1, Anna Svirina 1,
Georg Krainer 1,2,*, Michael Schlierf 1,3*

Affiliations:
1 B CUBE – Center for Molecular Bioengineering, TU Dresden, Tatzberg 41, 01307 Dresden, Germany
2 Centre for Misfolding Diseases, Yusuf Hamied Department of Chemistry, University of Cambridge, Lensfield Road, CB2 1EW Cambridge, UK
3 Cluster of Excellence Physics of Life, TU Dresden, 01062 Dresden, Germany 

§ Contributed equally to this work.
*To whom correspondence should be addressed: michael.schlierf@tu-dresden.de (M.S.), gk422@cam.ac.uk (G.K.)


Key words:
chaperones, outer membrane protein biogenesis, single-molecule FRET, protein folding, disaggregation, nanosecond microsecond and millisecond dynamics


Description:
This collection contains all raw TCSPC data for the study of the interaction of OmpX with chaperones SurA and Skp3. The data was collected on a custom-built confocal TCSPC instrument as described in Hartmann and Krainer et al. Molecules 2014 and Hartmann and Krainer et al. Analytical Chemistry 2015.For data details see comment.txt. Raw data was collected mainly by Neharika Chamachi and Andreas Hartmann.