![]() The infrared structure of PTH, however, did not reveal any bands at 1,632 and 1,682 cm. Unequivocal assignment of the ellipticity band at 222 mμ to helical structure is difficult due to the possible overlap of CD bands arising from β structure or aromatic chromophores. This degree of ellipticity if due to the peptide bond in an α helical configuration, suggests that PTH has a helical content of 10 – 15% or approximately 3 turns of helix in aqueous solution. The molar ellipticity at 222 mµ, the peak of the n → II * transition of the peptide band in α helical peptides is 3,000. The major dichroic activity of PTH in aqueous solution is centred near 200 mµ, the CD band which is characteristic of the disordered form of the peptide chromophore ( Beychok, 1966). ![]() The circular dichroic spectra of PTH is reproduced in Fig. The secondary structure (random coil, β or helical structure) of bovine PTH was evaluated by circular dichroism (CD) and infrared spectroscopy. ![]()
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. Archives
May 2023
Categories |