Q:Measurement of protein's surface hydrophobicity?

lgbell at liverpool.ac.uk lgbell at liverpool.ac.uk
Fri Feb 21 11:30:16 EST 1997


Achim Recktenwald, PhD wrote:
> 
> We want to change the surface hydrophobicity of several proteins through
> chemical modifications.
> 
> My problem now is to find a method which allows me to measure the
> protein's hydrophobicity and the changes achieved. So far, the best
> solution I could come up with is to perform reversed-phase
> chromatography. I would use the elution-shift during the gradient from
> aqueous to organic solvent as a value for the change in hydrophobicity.
> 
> But I assume, I am not the first one to have this problem. Any better
> methods available ?
> 
> Thanks for any hint.
> 
> Achim
> 
> P.S. Please email me an answer, as well (achim at ibex.ca); our
> service-provider has too often problems with the usenet-server.
> 
> _____________________________
> Achim Recktenwald, PhD
> IBEX Technologies, Inc.
> 5485 rue Pare
> Montreal, PQ, H4P 1P7
> Canada
> 
> Phone: (514) 344-4004
> Fax  : (514) 344-8827
> email: achim at ibex.ca

You could try ANS fluorescence studies.  This dye (anilino naphthalene 
sulfate, I think is its full name) binds to hydrophobic patches on the 
protein surface, on doing so a measurable fluorescence change occurs in 
its emittance.  I have seen several papers which have used this method to 
determine protein hydrophobicity.  Perhaps a medline search would turn up 
the relevant details.

Hope this helps,
Len Bell.
University of Liverpool. Uk
lgbell at liv.ac.uk



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