Hi,
I have not worked with this situation.
However, I agree that binding kinetics should be known (on and off
rates) and a majority of bound complex should exist over time, otherwise
the situation might be tricky since some contribution from unbound
protein might arise (with a shorter correlation time, and potentially
different dynamics). Also, contribution from potential conformational
exchange caused by binding and unbinding of the ligand (depending on the
exchange rate, i.e. on and off rates), rather than 'real' changes in
dynamics on the protein, could complicate analysis and give a false
impression of changes in the protein dynamics.
I hope this helps.
Best regards,
Séb :)
On 11-02-24 10:45 AM, Edward d'Auvergne wrote:
Hi,
This can be tricky. Can you estimate the percentage of monomer verses
dimer? Can you also estimate the amount of time the peptide binds to
the receptor? Do you have binding data for the NMR sample conditions?
If the more than 90% of the receptor is bound to the peptide and the
time bound to the receptor is significant, then you should be able to
handle this with standard model-free analysis using a single diffusion
tensor. This will likely require data at 2 or more field strengths.
Seb, have you worked with this situation?
Regards,
Edward
On 23 February 2011 11:04, Maddy Strickland<m.strickl...@bristol.ac.uk> wrote:
Hi everyone,
I'm moving on to looking at dynamics of binding to a receptor which I've
already studied using Relax for Lipari-Szabo data. I was wondering if I
added some unlabelled peptide to the 15n receptor how I could study the
new relaxation data? Can I still use Relax and the same pulse sequences
etc. or do I need a program specific to binding? It's a fairly strong
binder, but it would render the receptor more of a cylinder than a
sphere... What do you all think?
Madeleine Strickland
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--
Sébastien Morin, Ph.D.
Postdoctoral fellow
S. Grzesiek NMR Laboratory
Biozentrum, Universität Basel
Basel, Switzerland
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