FTIR spectroscopy study of PTHrP(1-34) involved in humoral hypercalcaemia of malignancy.

Abstract

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.

• Authors: D R McFarlane, E F McFarlane, J A Barden, B E Kemp
• Journal: Biochimica et biophysica acta (Biochim Biophys Acta) Vol. 1162 Issue 1-2 Pg. 187-94 (Mar 05 1993) ISSN: 0006-3002 [Print] Netherlands
• PMID: 8448183 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Amides
• Neoplasm Proteins
• Parathyroid Hormone
• Parathyroid Hormone-Related Protein
• Peptide Fragments
• Proteins
• Teriparatide
• parathyroid hormone-related protein (1-34)

Topics

• Amides (chemistry)
• Amino Acid Sequence
• Humans
• Hypercalcemia (blood, etiology)
• Molecular Sequence Data
• Neoplasm Proteins (chemical synthesis, chemistry)
• Parathyroid Hormone (chemical synthesis, chemistry)
• Parathyroid Hormone-Related Protein
• Peptide Fragments (chemical synthesis, chemistry)
• Protein Structure, Secondary
• Proteins
• Spectrophotometry, Ultraviolet (methods)
• Teriparatide