What about proteins where the crystals don't diffract well? I've found
in my teaching experience that students take your advice much more
seriously when they see it work on 3.5A data than they do when they see
it work on 1.5 A data.
-James Holton
MAD Scientist
On 6/17/2021 7:40 AM, Tanner,
Dear colleagues,
I have an opening for a postdoctoral fellowship in my group at Linköping
university, Sweden. The aim of the project is to study the evolutionary
relationship and structural and functional repurposing of human proteins
acquired by picornaviruses, building on research already
Is your enzyme monomeric or multimeric?
What time exactly does it mean when you say unprocessed substrate versus
processed?
What are your error margins (no error bars evident on your plots)?
Depending on your errors, your second plot is not a 'steep decline' but
instead could be a constant line.
Hello, you could also try:
http://www.ic50.tk/kmvmax.html
Or
http://ic50.org/kmvmax.html
The former has an exponential decay thing that might help with your substrate
inhibition and other things if you have biphasic behaviour ;-0
Cheers, Jon.C.
Sent from ProtonMail mobile
Original
For sure, you will need to collect data at lower substrate concentration to
determine what is going on for processed substrate. One should also
consider how the "initial rates" are measured. Ideally, the amount of
substrate depleted during the initial rate measurement should be less that
5%. When
Dear Prem,
I agree entirely with Tristan's conclusion that the processed substrate is also
acting as an inhibitor at higher concentrations. You would need to run an
experiment with a wider range of concentrations used (especially lower
concentrations) to get a better feel for the range of the
Hi Prem,
The immediate problem here is that the curve for the processed substrate simply
cannot be described by simple Michaelis-Menten kinetics. Assuming the assay has
worked as expected, the declining rate with increasing substrate concentration
suggests to me that this substrate also acts
