Q:Measurement of protein's surface hydrophobicity?
Bill Van Antwerp
bvanantwerp at pacificnet.net
Mon Feb 24 16:22:24 EST 1997
"\"Uncle Al\" Schwartz" <UncleAl0 at ix.netcom.com> wrote:
>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 ?
>Plate the thing out on a glass microscope slide (maybe with silane
>coupling agent derivatization on the glass - Petrarch Systems) and
>measure the contact angle with water. Denaturation debates alone ought
>to be good for two or three communications plus a full paper.
Denaturation effects on a glass slides would indeed make a nice paper
A far better method, assuming that you have either tyrosines or tryptophans in the protein is to look at the fluorescence spectra as you modify the surface of the protein. e-mail me if you need some references or other such help.
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