FTIR spectroscopy study of PTHrP(1-34) involved in humoral hypercalcaemia of malignancy.
The components of secondary structure of the biologically-active N-terminal domain of human parathyroid-hormone-related protein (residues 1-34) and several truncated species were examined using Fourier transform infrared (FTIR) spectroscopy. The major structural features include a segment of alpha-helix within the N-terminal segment probably extending from Glu-4 to Lys-11 with three beta-turns localized to the segments Gly-12 to Ile-15, Gln-16 to Arg-20 and His-25 to Ala-29. Some beta-sheet was detected in the full-length peptide, but not in any of the C-terminal truncated samples. These structural features were studied in the smaller peptides for the purpose of localization of the various components and with a view to describing the region likely to form the bulk of the receptor binding site.
McFarlane
D R
DR
Department of Anatomy, University of Sydney, Australia.
McFarlane
E F
EF
Barden
J A
JA
Kemp
B E
BE
D000577:Amides / Q000737:chemistry; D000595:Amino Acid Sequence; D006801:Humans; D006934:Hypercalcemia / Q000097:blood / Q000209:etiology*; D008969:Molecular Sequence Data; D009363:Neoplasm Proteins / Q000138:chemical synthesis / Q000737:chemistry*; D010281:Parathyroid Hormone / Q000138:chemical synthesis / Q000737:chemistry*; D044162:Parathyroid Hormone-Related Protein; D010446:Peptide Fragments / Q000138:chemical synthesis / Q000737:chemistry*; D017433:Protein Structure, Secondary; D011506:Proteins; D013056:Spectrophotometry, Ultraviolet / Q000379:methods; D019379:Teriparatide
D000577:Amides; D009363:Neoplasm Proteins; D010281:Parathyroid Hormone; D044162:Parathyroid Hormone-Related Protein; D010446:Peptide Fragments; D011506:Proteins; D019379:Teriparatide; C054296:parathyroid hormone-related protein (1-34)