Single Peptide Bonds Exhibit Poly(Pro)II (“Random Coil”) Circular Dichroism Spectra
Isa Gokce, Robert W. Woody, Gregor Anderluh, Jeremy H. Lakey
The far-UV circular dichroism spectra of a series of amino acid derivatives containing single peptide bonds have been measured. The N-acetyl-alanine displays a polyproline (PP) II-like spectrum, but alaninamide shows a very weak positive signal. Similarly Gly-Ala shows a PPII spectrum, but Ala-Gly does not. On heating, the spectrum shows a two-state transition also shown by long PPII polypeptides. Thus the characteristic PPII negative maximum at <200 nm results from the coupling of a peptide bond N-terminal to the chiral α-carbon, and therefore the simplest peptide bonds have a preferred conformation that defines the spectrum of disordered proteins of any size.
Circular dichroism, Secondary structure, Biochemistry