I was wondering - why is imidazole bad for proteins?
I've always heard that high concentrations are "bad" for proteins, but a bit of googling did not reveal the answer. Does it actually react with side chains, or cause unfolding/aggragation? Just wondering... Good tip with the His-SELECT media - thanks Artem! Ed ______________ T.Edwards Ph.D. Garstang 8.53d Astbury Centre for Structural Molecular Biology University of Leeds, Leeds, LS2 9JT Telephone: 0113 343 3031 <http://www.bmb.leeds.ac.uk/staff/tae/> http://www.bmb.leeds.ac.uk/staff/tae/ <http://www.bmb.leeds.ac.uk/staff/tae/Research> "The doubter is a true man of science; he doubts only himself and his interpretations, but he believes in science". ~Claude Bernard ________________________________ From: CCP4 bulletin board [mailto:[EMAIL PROTECTED] On Behalf Of Jacob Keller Sent: 18 July 2008 01:04 To: CCP4BB@JISCMAIL.AC.UK Subject: [ccp4bb] Imidazole's ability to chelate metal ions Dear Crystallographers, Does anybody happen to know whether imidazole is able to chelate metal ions in solution? It seems reasonable that since it can compete for binding to IMAC resins, it should have some affinity for at least Ni++ and Co++, but what about metal ions like Ca++ and Mg++? I assume that the affinity is weak, but at the concentrations at which we are wont to use it in our elutions (~100-500 mM), does it not seem likely that other metal ions are being competed away from our proteins as well? Jacob Keller ******************************************* Jacob Pearson Keller Northwestern University Medical Scientist Training Program Dallos Laboratory F. Searle 1-240 2240 Campus Drive Evanston IL 60208 lab: 847.491.2438 cel: 773.608.9185 email: [EMAIL PROTECTED] *******************************************
