Abstract
It has been shown that in aqueous solution histone H1 and H5 C-terminal fragments and peptide hormones β-endorphin and ACTH adopt preferably the left-handed helical conformation of the poly-l-proline II type. Scanning microcalorimetry and circular dichroism have been used to show that the linear temperature dependence of CD maximum amplitude and partial heat capacity value are broken in the temperature interval between 50 and 60°C, after which [C]p reaches the constant level. It was proposed to be due to noncooperative disordering of the conformation caused by the destruction of the polypeptide hydration shell.
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Makarov, A.A., Adzhubei, I.A., Protasevich, I.I. et al. Scanning microcalorimetry and circular dichroism study of melting of the natural polypeptides in the left-handed helical conformation. J Protein Chem 12, 85–91 (1993). https://doi.org/10.1007/BF01024919
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DOI: https://doi.org/10.1007/BF01024919