[Microcalorimetric study of polypeptides in the conformation of the left helix of the poly-L-proline II type].
Nonuniform size distribution of nascent globin peptides, evidence for pause localization sites, and a contranslational protein-folding model.
Natural polypeptides in left-handed helical conformation. A circular dichroism study of the linker histones' C-terminal fragments and beta-endorphin.
[Study of the conformational properties of C-terminal fragments of histones H1, H5, and beta-endorphin by circular dichroism].
Scanning microcalorimetry and circular dichroism study of melting of the natural polypeptides in the left-handed helical conformation.
