I recorded far UV CD spectra for two of my proteins and their complex. Both proteins mainly contain beta sheets connected by loops. The protein (say A)which has no alpha helix gave minima around 205nm. The protein (say B) which has one small helix gave minima around 215nm. And their complex (say AB) showed minima close to 230nm. Except the shift the remaining spectra looks almost same. Previous crystallographic studies with complex of similar proteins showed no considerable change in sec. structure. What could be explanation for the shift to 230nm?
Is there a shift in the absorption spectrum? Complexation can lead to red shifts in the optical spectrum.
In relation to CD? I do not know any immediately. I gave this answer more as an idea than a definite explanation. Such redshifts are common for small molecules, but it is unclear if that scales to large protein systems.
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