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

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

  • Biochim Biophys Acta. 1993 Mar 5;1162(1-2):187-94. doi: 10.1016/0167-4838(93)90146-i.
D R McFarlane 1,  E F McFarlane,  J A Barden,  B E Kemp
Affiliations

Affiliation

  • 1 Department of Anatomy, University of Sydney, Australia.
PMID: 8448183 DOI: 10.1016/0167-4838(93)90146-i
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.

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