Hi CD experts
I'm working on a typical beta-sheet protein. So the CD spectrum displays a
minimum at about 218 nm and the curve crosses the x-axis at about 200 nm.
Now, when we analyze the protein after a period of heat exposure we see
an increase of the amplitude: so the spectrum does not shift but only the
ellipticity increases. Does anyone know how to interprete this result? Does
this result indicate that the amount of random coil increases upon heating?
Thanks in advance for your comments
Ronald Smulders, The University of Nijmegen
