Hi out there,
I am trying to interpret the UV-difference spectra of a native enzyme
with two differently denatured states. One state is obtained at pH 3.0, the
other by removing a Zn atom which seems to be essential for stabilizing the
native state.
In both cases I get nice peaks in the difference spectrum (denat - native)
at 299 and 286 nm, respectively. The first spectrum, however is negagtive,
the second positive.
The appearance of the peaks tell me that the only Trp residue seems to get
into a more hydrophobic environment.
But what does the fact of getteing either a positive or a negative peak
tells me?
Is there any good literature available dealing with this matter?
Thanks for any help!
Tilman
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Tilman Voss Ph.D.
Protein Chemistry Group
Bender+Co
Vienna, Austria
Tel: xx43-1-80105 351
Fax: xx43-1-80105 366
Email: VOSS at AIMP.UNA.AC.AT
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