Simonetti M, Falcigno L, Paolillo L, Di Bello C
Department of Chemical Process Engineering, University of Padova, Italy.
Biopolymers. 1997 Apr 5;41(4):461-79. doi: 10.1002/(SICI)1097-0282(19970405)41:4<461::AID-BIP10>3.0.CO;2-L.
Synthetic peptides of different size, reproducing the proteolytic processing site of proocytocin, were studied by CD under several experimental conditions in order to ascertain the ability of different solvents to stabilize secondary structural motifs, such as alpha-helix tracts and beta-turns. A combination of deconvolution methods and empirical calculations subtracting the contributions due to unordered structures from the spectra suggests that in solution (a) mainly two distinct families of ordered conformers containing structurally different beta-turns are present, (b) the relative stability of the different conformers depends from the nature of the solvent, and (c) in the case of the larger peptides, a population containing an alpha-helical conformation is also present. From the biological point of view the presence of at least two families of ordered conformers could be in line with current theories assuming that the catalytic effect of the receptor microenvironment may be determinant in shifting the equilibrium toward the active conformation.
