Single peptide bonds exhibit poly(pro)II ("random coil") circular dichroism spectra.
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 alpha-carbon, and therefore the simplest peptide bonds have a preferred conformation that defines the spectrum of disordered proteins of any size.
Institute of Cell and Molecular Biosciences, University of Newcastle-upon-Tyne, Framlington Place, Newcastle-upon-Tyne NE2 4HH, UK.
Isa
I
Gokce
Robert W
RW
Woody
Gregor
G
Anderluh
Jeremy H
JH
Lakey
D002942:Circular Dichroism; D010455:Peptides / Q000737:chemistry*; D011392:Proline / Q000737:chemistry*; D013696:Temperature
D010455:Peptides; D011392:Proline