| Range |
10 to 30 Fold
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Pielak GJ, Li C, Miklos AC, Schlesinger AP, Slade KM, Wang GF, Zigoneanu IG. Protein nuclear magnetic resonance under physiological conditions. Biochemistry. 2009 Jan 20 48(2):226-34. p.227 right column 2nd paragraphPubMed ID19113834
|
| Primary Source |
20) Mullineaux CW, Nenninger A, Ray N, Robinson C. Diffusion of green fluorescent protein in three cell environments in Escherichia coli. J Bacteriol. 2006 May188(10):3442-8. AND (21) Elowitz et al., Protein mobility in the cytoplasm of Escherichia coli. J Bacteriol. 1999 Jan181(1):197-203. AND (22) Zhou HX, Rivas G, Minton AP. Macromolecular crowding and confinement: biochemical, biophysical, and potential physiological consequences. Annu Rev Biophys. 2008 37 375-97.PubMed ID16672597, 9864330, 18573087
|
| Method |
Using fluorescence to measure the translational diffusion of
GFP, either by itself or fused to other proteins. |
| Comments |
Whereas the
eukaryotic cytoplasm slows diffusion no more than 4-fold (BNID 106192),
the cytoplasm of E. coli slows diffusion 10-30-fold (primary sources). Please note that attachment of GFP to the protein of interest adds 27
kDa of bulk to the target protein, and provides information
only about the environment of the fluorophore, which
occurs only once in the target protein. |
| Entered by |
Uri M |
| ID |
106193 |