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

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An Erratum to this article was published on 01 September 1986

Summary

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.

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Authors and Affiliations

  1. Laboratory for the Study of Skeletal Disorders and Rehabilitation, Department of Orthopedic Surgery, Harvard Medical School and Children's Hospital, 300 Longwood Avenue, Boston, Massachusetts 02115

    V. Renugopalakrishnan, A. Uchiyama, M. Suzuki, B. Lefteriou & M. J. Glimcher

  2. Department of Biochemistry, The University of Texas Health Sciences Center, San Antonio, Texas

    P. M. Horowitz

  3. National Institute on Drug Abuse, Rockville, Maryland

    R. S. Rapaka

Authors
  1. V. Renugopalakrishnan
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  2. A. Uchiyama
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  3. P. M. Horowitz
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  4. R. S. Rapaka
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  5. M. Suzuki
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  6. B. Lefteriou
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  7. M. J. Glimcher
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Additional information

An erratum to this article is available at http://dx.doi.org/10.1007/BF02555205.

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Renugopalakrishnan, V., Uchiyama, A., Horowitz, P.M. et al. Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by Circular Dichroism and Fourier Tranform-Infrared Spectroscopy. Calcif Tissue Int 39, 166–170 (1986). https://doi.org/10.1007/BF02555113

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  • DOI: https://doi.org/10.1007/BF02555113

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