Resolution of conformation equilibria in linear peptides by circular dichroism in cryogenic solvents.
The circular dichroism spectra of the synthetic peptide antigen, 209-222 of the surface glycoprotein of the rabies virus were recorded as a function of solvent composition and over the temperature range of +60 degrees C to -135 degrees C; beta-III and beta-II reverse turn conformations were found to exist in TFE/H2O (3:1) at room temperature and in ethanediol/H2O (2:1) below -110 degrees C respectively. Evidence, from comparison of observed and calculated spectra, is given to support the existence of a conformational equilibrium between a beta-II and a beta-III reverse turn. These data can serve as a basis for synthetic vaccine development and understanding the nature of polypeptide chain folding.
D002942:Circular Dichroism; D006023:Glycoproteins / Q000378:metabolism; D009498:Neurotoxins / Q000378:metabolism; D010446:Peptide Fragments; D011487:Protein Conformation; D011819:Rabies Vaccines / Q000302:isolation & purification; D011820:Rabies virus; D011950:Receptors, Cholinergic / Q000378:metabolism; D012997:Solvents; D013696:Temperature; D014764:Viral Proteins / Q000378:metabolism
D006023:Glycoproteins; D009498:Neurotoxins; D010446:Peptide Fragments; D011819:Rabies Vaccines; D011950:Receptors, Cholinergic; D012997:Solvents; D014764:Viral Proteins