Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by Circular Dichroism and Fourier Tranform-Infrared Spectroscopy

V. Renugopalakrishnan, A. Uchiyama, P. M. Horowitz, R. S. Rapaka, M. Suzuki, B. Lefteriou, M. J. Glimcher

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

The secondary structures of two phosphoproteins from chicken bone matrix of Mr ≈15kDa and ≈28kDa, rich in Asx, Glx, and Ser, and containing Ser(P) and Thr(P) residues, have been investigated in solution by Circular Dichroism (CD) and Fourier Transform-Infrared Spectroscopy (FT-IR). CD spectroscopy, which yields useful information on the backbone conformation of polypeptides and proteins, suggests a predominantly β-sheet structure for the two phosphoproteins. The FT-IR spectra of the ≈15kDa protein, which is sensitive to secondary structure and hence provides complimentary information to CD spectroscopy, are consistent with the results obtained by CD studies.

Original languageEnglish (US)
Pages (from-to)166-170
Number of pages5
JournalCalcified tissue international
Volume39
Issue number3
DOIs
StatePublished - May 1986
Externally publishedYes

Keywords

  • CD studies of bone phosphoproteins
  • Extended β-sheet structure for bone phosphoproteins
  • FT-IR studies of bone phosphoproteins
  • Secondary structure of bone phospho-proteins

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism
  • Orthopedics and Sports Medicine
  • Endocrinology

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