Hi all!
I am a novice with protein unfolding problems and am facing a strange
problem:
I wanted to unfold my protein with guanidium chloride. As a test, I
added some protein (25 ug/ml) to 4 M guanidium in 20 mM tris ph 7.5.
When I meaured fluorescence, the native protein gave a good signal, so
did a small signal for the blank (buffer + 4 M guanidium).
However, on with the test (protein+ 4 M guanidium), I got a perfect
straight line at 0 intensity units. I wonder what's wrong? Any
suggestions?
Thanks in advance for all help,
Bhupesh. 9-5-00.
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* Bhupesh Taneja, SRF (Graduate student) *
* Institute of Microbial Technology, *
* Sector 39-A, *
* Chandigarh - 160 036. (INDIA). *
* Ph: +91 172 695226 extn 494 *
* *
* Email : bhupesh at lion.imtech.ernet.in *
* bhupesht at yahoo.com *
http://www.bragg.imtech.ernet.in/bhupesh
* *
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