Analysis of protein folding by CD spectroscopy 

This was extremely helpful! Could you perhaps recommend extra resources that might be helpful in learning this technique and data interpretation

We have a protein sample, which is being used at different temperatures and pH and we are seeing vertical (i.e., molar ellipticity magnitude) shifts in the CD spectrum. It cannot be due to concentration because it is all the exact same sample. We did a 222nm/208 and for the most part there is linearity across temperatures at pH 7. However, at lower pH the 222nm/208nm plots show kinks at the higher temps, but there is no "directionality"/correlation between the magnitude of the vertical shift and temperature (or pH). The shifts seem quite random. Any advice? Suggestions? Should we do WSD to be able to say "There is no significant change in secondary structure?"

how did you do it can you share with me , thank you

Can you post the link for the normalization software that is at 16:45?

I can't see clearly nd this vid is too helpfull.

the video image is too poor, you need to fix it more