Published August 24, 2019
| Version v1
Journal article
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Resolving dynamics and function of transient states in single enzyme molecules - Dataset
Creators
- 1. University Wuerzburg, Rudolf-Virchow Center for Experimental Biomedine, Molecular Microscopy
- 2. Heinrich-Heine University Duesseldorf, Institute of Molecular Physical Chemistry
- 3. Clemson University, Single Molecular Biophysics lab
- 4. Jules Stein Eye Institute and Department of Chemistry and Biochemistry, University of California
- 5. UCSF Department of Bioengineering and Therapeutic Sciences
- 6. Heinrich-Heine University Duesseldorf, Institute for Pharmaceutical and Medical Chemistry
Description
Original measurement data of:
Resolving dynamics and function of transient states in single enzyme molecules
Hugo Sanabria, Dmitro Rodnin, Katherina Hemmen, Thomas Peulen, Suren Felekyan, Mark R Fleissner, Mykola Dimura, Felix Koberling , Ralf Kühnemuth, Wayne Hubbell, Holger Gohlke, Claus A.M. Seidel
4 different subfolders:
- Original EPR-data
- Original ensemble fluorescence data measured in cuvettes by time-correlated single-photon counting
- Original single-molecule fluorescence data
- Original single-molecule fluorescence data used to characterize variants with modified functionality to understand the enzymes function
Additionally the results of FRET screening for all selected PDB structures of T4L are provided.
Notes
NIH (grant R01EY05216 to WLH),
NSF CAREER MCB (grant 1749778 to HS)
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Description_of_uploaded_data.pdf
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Additional details
Related works
- Is cited by
- Journal article: 10.1038/s41467-020-14886-w (DOI)