[RASMB] Empty voids

Richard Kingston rl.kingston at auckland.ac.nz
Thu Jun 3 17:35:25 PDT 2010


Hi Dave

To achieve a full thermodynamic characterization of  protein stability is fairly arduous. But you could get a good idea of the relative stabilities of any mutants by following the temperature-induced unfolding of the proteins spectroscopically (e.g. using CD or  Fluorescence). Comparison with the wild-type protein would give you a pretty decent idea of how much each  mutation was costing you. Although this will not give you the complete thermodynamic information that DSC does (it's very difficult to estimate the heat capacity changes associated with protein unfolding using this kind of spectroscopic approach) it's fast, and much less heavy on material.

Best Regards,

Richard

Richard Kingston, PhD.
School of Biological Sciences
The University of Auckland
New Zealand
website: http://persephone.sbs.auckland.ac.nz/richard/lab/


On 4/06/2010, at 4:08 AM, Dj Scott wrote:

> Hello all in RASMB-land.
> A question for you.
>  
> If I make a void in a protein by mutating a larger residue to a smaller one in the hydrophobic core, what is the thermodynamic cost of this, and how would it be best to measure it.
>  
> All thoughts welcome.
> Best
>  
> Dave.
> >>>>>>>>>>>>>>>>>>>>>>>>>> 
> Dr. David J. Scott 
> Associate Professor in Physical Biochemistry 
> National Centre for Macromolecular Hydrodynamics 
> School of Biosciences 
> University of Nottingham 
> Sutton Bonington Campus 
> Leicestershire. LE12 5RD. 
> United Kingdom. 
> Phone: +44 (0) 115 951 6221 
> Fax: +44 (0) 115 951 6142 
> Email: dj.scott at nottingham.ac.uk 
> Web: www.nottingham.ac.uk/ncmh
> 
>  
> 
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