protein, protein dimerization, buffers role, salts role in proteins precipitation, proteomics, protein crystallography
Buffer conditions like pH, ionic strength and temperature as well as the use of divalent salt could all have impacts on the oligomerisation state of protein. What is the protein that you are working on and what is your buffer condition? In the end, it all depends on the nature of your protein~
thanks
i need some articles where specifically sodium citrate is used for purification.
Hi Najeeb, there are about 500, 000 articles on citrate and protein purification on Google scholar.
https://scholar.google.com/scholar?hl=en&q=citrate+protein+purification&btnG=&as_sdt=1%2C21&as_sdtp=
I think you will have to limit the search of what you at looking for.
yea i searched the same but didnt got a single article on citrate except an article that gives some clue about citrate role in protein purification.
thanks for your time
Is your protein a basic one? Citrate could make intermolecular bridges involving positive charges. Also its chelating activity can be important, as Steingrimur pointed out.
Citrate is not only a good buffer in the slightly acidic range (pH 2-6) and a chelating agent for bivalent metals, it is also a cosmotrope (right side of the Hofmeister series of anions) that stabilises protein structure.
to follow up on Englebert's statement, ZhenYang in Journal of Biotechnology
Volume 144, Issue 1, 12 October 2009, Pages 12-22 describes a Gouvea et al. (2006) paper which "observed a significant activation of poliovirus picornain-3C protease (up to 104-fold) by a series of anions following the Hofmeister series: citrate3− > SO42− > HPO42− > acetate− > HCO3− > Cl−, which was reflected by an increase in kcat and no significant change in Km. This salt-induced activation is associated with conformational changes as demonstrated by structural studies using fluorescence and circular dichroism."
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