pi->pi* transitions are seen by a positive intensity around 190-195 ('perpendicular') and a negative intensity around 208 ('parallel') in alpha helices. I have a protein that displayed a helical style profile where the pi->pi* perpendicular (190-195) is much more intense and there is minimal pi->pi* parallel intensity (208). What conformation is likely to cause this and why? It would help to know where on the peptide backbone these transitions are taking place and why they would be more prevalent on certain structures.
Philippe Roger Bovy
Like pi>pi interactions occuring between aromatic side chains, is It ?
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