| Range |
2-3 times slower
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Theillet FX et al., Physicochemical properties of cells and their effects on intrinsically disordered proteins (IDPs). Chem Rev. 2014 Jul 9 114(13):6661-714. doi: 10.1021/cr400695p p.6668 left column 3rd paragraphPubMed ID24901537
|
| Primary Source |
[177] Ye Y et al., (19) F NMR spectroscopy as a probe of cytoplasmic viscosity and weak protein interactions in living cells. Chemistry. 2013 Sep 16 19(38):12705-10. doi: 10.1002/chem.201301657PubMed ID23922149
|
| Method |
Primary source abstract: "Herein, [investigators] demonstrate the use of (19) F NMR [Nuclear magnetic resonance] spectroscopy to measure cytoplasmic viscosity and to characterize nonspecific protein-protein interactions in living Escherichia coli cells." |
| Comments |
P.6668 left column 3rd paragraph: "In E. coli, rotational diffusion was found to be 2–3 times slower than in pure water (primary source)." Primary source abstract: "[Investigators] found that sample inhomogeneity has a negligible effect on resonance broadening, the cytoplasmic viscosity is only about 2-3 times that of water, and ubiquitous transient weak protein-protein interactions in the cytosol play a significant role in governing the detection of proteins by using in-cell NMR spectroscopy." |
| Entered by |
Uri M |
| ID |
115861 |