| Range |
~90 %
|
| Organism |
Bacteria Escherichia coli |
| Reference |
Kyne C et al., Protein charge determination and implications for interactions in cell extracts. Protein Sci. 2017 Feb26(2):258-267. doi: 10.1002/pro.3077 p.259 left column top paragraphPubMed ID27813264
|
| Primary Source |
[27] Spitzer J, Poolman B. The role of biomacromolecular crowding, ionic strength, and physicochemical gradients in the complexities of life's emergence. Microbiol Mol Biol Rev. 2009 Jun73(2):371-88. doi: 10.1128/MMBR.00010-09PubMed ID19487732
|
| Comments |
P.259 left column top paragraph: "While the paucity of proteins with pIs [Isoelectric points] between pH 7.4–7.6 is universal, the relative abundance of cationic and anionic proteins varies according to species and subcellular location [ref 28]. Approximately 90% of the most abundant proteins in the E. coli cytoplasm are anionic at physiological pH suggesting that charge–charge repulsion is critical in stabilising the cytoplasm against random aggregation [primary source]." |
| Entered by |
Uri M |
| ID |
114103 |