to complement the very nice description by jeremy, you may wish to try
and decompose the vibrational modes to get this sense by focussing on
the origins of the "red shift" in the vibrational spectrum and this
accounts largely for the increased vibrational entropies upon
complexation. This
if the link between the domains is not part of the interface then perhaps
a good first approximation may be to "cut" the linker and then use a
program such as APBS to compute the binding energy..
> Hi,
>
> Recently we determined two structures of the same protein in complex with
> different molec
Dear all
Can anyone suggest examples where the same peptide is bound to the same
receptor site in two or more different (very different) conformations
and this binding has been resolved crystallographically as well as using
ITC. In the extreme cases this could be two different proteins as well
An extension of this topic: does anyone know of examples where for
complexes between the two proteins A and B, protein A has two different
conformations at its interface?
thanks
chandra
-Original Message-
From: CCP4 bulletin board [mailto:ccp...@jiscmail.ac.uk] On Behalf Of
Aaron O
hi
yes this may happen in some circumstanceshave a look at
J Am Chem Soc. 2008 Oct 15;130(41):13514-5.
> Hi,
>
> I had a question about flexibility in ligand binding in an enzyme active
> site. Is it possible for a substrate/product analogue to bind in more
> than
> one conformation in the
