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Abstract
The solution structures of two human growth hormone releasing factor analogues, 27Leu 45Gly-hGHRF(1–45)OH and 27Nle-hGHRF(1–29)NH 2, are investigated by means of circular dichroism and nuclear magnetic resonance spectroscopy. Using circular dichroism spectroscopy, it is shown that both peptides adopt ordered structures at low concentrations of trifluoroethanol (~30%). Quantitative analysis of the circular dichroism spectra indicates that the same number of residues, approximately 23 to 25, are in a helical state in both peptides. Using two-dimensional nuclear magnetic resonance methods all proton resonances of the 27Nle-hGHRF(1–29)NH 2 fragment are assigned and its secondary structure is determined from a qualitative interpretation of the nuclear Overhauser enhancement data. Two distinctive regions of α-helix are present extending from residues 6 to 13 and 16 to 29.
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