On Tue, 2012-10-30 at 16:12 +, Peter Hsu wrote:
I'm wondering, since I lack activity at this pH point, would it lead
to no binding of a substrate analog?
Not necessarily. You should check pH dependence of the Km - it might be
that lower activity is primarily due to reduction in kcat.
Hi all,
I'm working on a protein that I recently got crystals of. My functional studies
show that the protein has optimal activity at lower pHs, while losing 90%
activity at about pH8. I've been trying to soak/cocrystallize a substrate
analog (small molecule) into my crystals (grown at ~pH8)
, October 30, 2012 5:13 PM
To: CCP4BB@JISCMAIL.AC.UK
Subject: [ccp4bb] oof topic: pH effect on substrate analog
Hi all,
I'm working on a protein that I recently got crystals of. My functional
studies show that the protein has optimal activity at lower pHs, while
losing 90% activity at about pH8
...@u.washington.edu
To: CCP4BB@JISCMAIL.AC.UK
Sent: Tuesday, October 30, 2012 12:12:58 PM
Subject: [ccp4bb] oof topic: pH effect on substrate analog
Hi all,
I'm working on a protein that I recently got crystals of. My functional studies
show that the protein has optimal activity at lower pHs, while
To: CCP4BB@JISCMAIL.AC.UK
Sent: Tuesday, October 30, 2012 12:12:58 PM
Subject: [ccp4bb] oof topic: pH effect on substrate analog
Hi all,
I'm working on a protein that I recently got crystals of. My functional studies
show that the protein has optimal activity at lower pHs, while losing 90%
activity