From: Jo Butler <pjgb@mrc-lmb.cam.ac.uk>
  To  : Brian M. Baker <baker@xtal200.harvard.edu>
  Date: Mon, 20 Nov 2000 13:18:53 +0000

Re: affinities vs. temperatures

Dear Brian,

Yes - the protein aggregation of TMV protein is entropically driven and 
therefore increases with temperature.  A paradigm example is a protein 
solution (say 5 mg/ml) at pH 5.0, which will be clear (the lowest 
aggregation state, "A-protein") at 0° but goes cloudy (long protein 
helices) on warming to 20°.

Jo

--On Sunday, November 19, 2000 11:32 pm -0500 "Brian M. Baker" 
<baker@xtal200.harvard.edu> wrote:

> Greetings all,
> This is highly off-topic and I apologize, but does anybody know of any
> well-characterized examples of protein-ligand (or oligomerization)
> interactions in which the equilibrium constant increases (binding becomes
> tighter) with temperature?
> Thanks and have good day!
> -Brian
>
>
============================================
> Brian M. Baker
> Department of Molecular and Cellular Biology
> Harvard University
> baker@crystal.harvard.edu
> (617) 496-6074
>
>



P.J.G. Butler,
MRC Laboratory of Molecular Biology,
Hills Road, Cambridge, CB2 2QH, UK.
Tel. +44 (0)1223 402296