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°C to -135°C; β-III and β-II reverse turn conformations were found to exist in TFE H2O (3:1) at room temperature and in ethanediol/H2O (2:1) below -110°C respectively. Evidence, from comparison of observed and calculated spectra, is given to support the existence of a conformational equilibrium between a β-II and a β-III reverse turn. These data can serve as a basis for synthetic vaccine development and understanding the nature of polypeptide chain folding. © 1987.
Siligardi, G., Drake, A.F., Mascagni, P., Neri, P., Lozzi, L., Niccolai, N., et al. (1987). Resolution of Conformational Equilibria In Linear Peptides By Circular-dichroism In Cryogenic Solvents. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 143(3), 1005-1011 [10.1016/0006-291X(87)90351-2].
Resolution of Conformational Equilibria In Linear Peptides By Circular-dichroism In Cryogenic Solvents
Lozzi L.;Niccolai N.;
1987-01-01
Abstract
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°C to -135°C; β-III and β-II reverse turn conformations were found to exist in TFE H2O (3:1) at room temperature and in ethanediol/H2O (2:1) below -110°C respectively. Evidence, from comparison of observed and calculated spectra, is given to support the existence of a conformational equilibrium between a β-II and a β-III reverse turn. These data can serve as a basis for synthetic vaccine development and understanding the nature of polypeptide chain folding. © 1987.
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https://hdl.handle.net/11365/33640
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