Hi all,

I've limited experience interpreting CD spectra, so I might be missing 
something, but I've collected CD data for a hydrophobic 15-mer peptide that 
forms a putative alpha-helix. I get a region of strong negative ellipticity, 
bottoming out at ~222nm; however, I also get a strong positive peak (of equal 
magnitude to the 222nm minimum) at ~208nm. This 208 peak is opposite to a 
textbook alpha-helical spectrum (like it's been inverted).

>From what I've read, short alpha-heical peptides often lack 208nm minima, and 
>protonated carboxyl groups producce positive ellipticity at this wavelength; 
>however, apart from the C-terminus, I don't have any carboxyl groups, and the 
>peptide is in standard PBS buffer to boot. Any suggestions on what might be 
>causing this odd 208 peak? NOTE: current data isn't below 200nm.

Thanks!

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