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

doi:10.1007/BF02555113

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 journal › Article › peer-review

10 Scopus citations

Abstract

The secondary structures of two phosphoproteins from chicken bone matrix of M_r ≈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 language	English (US)
Pages (from-to)	166-170
Number of pages	5
Journal	Calcified tissue international
Volume	39
Issue number	3
DOIs	https://doi.org/10.1007/BF02555113
State	Published - May 1986
Externally published	Yes

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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10.1007/BF02555113

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Renugopalakrishnan, V., Uchiyama, A., Horowitz, P. M., Rapaka, R. S., Suzuki, M., Lefteriou, B., & Glimcher, M. J. (1986). Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by Circular Dichroism and Fourier Tranform-Infrared Spectroscopy. Calcified tissue international, 39(3), 166-170. https://doi.org/10.1007/BF02555113

Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by Circular Dichroism and Fourier Tranform-Infrared Spectroscopy. / Renugopalakrishnan, V.; Uchiyama, A.; Horowitz, P. M. et al.

In: Calcified tissue international, Vol. 39, No. 3, 05.1986, p. 166-170.

Research output: Contribution to journal › Article › peer-review

Renugopalakrishnan, V, Uchiyama, A, Horowitz, PM, Rapaka, RS, Suzuki, M, Lefteriou, B & Glimcher, MJ 1986, 'Preliminary studies of the secondary structure in solution of two phosphoproteins of chicken bone matrix by Circular Dichroism and Fourier Tranform-Infrared Spectroscopy', Calcified tissue international, vol. 39, no. 3, pp. 166-170. https://doi.org/10.1007/BF02555113

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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.",

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",

author = "V. Renugopalakrishnan and A. Uchiyama and Horowitz, {P. M.} and Rapaka, {R. S.} and M. Suzuki and B. Lefteriou and Glimcher, {M. J.}",

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AU - Uchiyama, A.

AU - Horowitz, P. M.

AU - Rapaka, R. S.

AU - Suzuki, M.

AU - Lefteriou, B.

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

Abstract

Keywords

ASJC Scopus subject areas

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