In E. coli rotational diffusion is slower than that in pure water by

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