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The apparent Ki is a macroscopic parameter; the interpretation of it,
whether a single binding event, or several, is microscopic. Multiple
binding of a ligand or inhibitor is measured in the same way.
yes, this is true; however, by fitting your kinetic data with models
accounting for either one or two or three binding sites, you will be
able to estimate which of these model is the most likely, and to
attribute a binding constant for each of your different binding sites ..
try using GOSA (Global Optimization by Simulated Annealing - http://
www.bio-log.biz/), which is a perfect fitting program for kinetic
(among others things); you can get a 15 days evaluation version for
free, yet the license is very cheap.. it will permit you to
characterize the number of binding sites of your ligand on your
protein, and to estimate the affinities of each of these binding sites.
You may look at Stojan et al., 2004 (Eur J. of Biochem), Frasco et
al. 2005 (Biomarkers), Fournier, 2005 (Chem Biol Interact), Siadat et
al.,2006 (BMC Biochem) or Colletier et al. 2006 (EMBO J.), etc,etc,
to see what you can do using this program
ciao,
Jacques-Ph
Le 17 sept. 06 à 14:17, Santarsiero, Bernard D. a écrit :
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The apparent Ki is a macroscopic parameter; the interpretation of it,
whether a single binding event, or several, is microscopic. Multiple
binding of a ligand or inhibitor is measured in the same way.
On Sun, September 17, 2006 1:24 am, Michael nelson wrote:
Sorry,this is a non-ccp4 problem.
I have a inhibitor that is able to bind to multiple positions in a
single
protein.Does anybody here know how to calculate or measure Kd or
ki of
such a molecule.
Many thanks
Mike.
