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Conformational studies of osteocalcin in solution.

Abstract:

1H-NMR and circular dichroism studies have been carried out on osteocalcin, a 49-residue, calcium-binding protein, the sequence of which contains a disulphide bridge, a proline-rich segment and three gamma-carboxyglutamic acid (Gla) residues. These latter residues have been proposed to lie on one face of an alpha helix and interact with the mineral phase, leading to incorporation of the protein into the bone matrix. Circular dichroism shows an increase in the alpha-helical structure on Ca2+ b...

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Publication status:
Published

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Authors


Atkinson, RA More by this author
Hauschka, PV More by this author
Levine, BA More by this author
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Journal:
European journal of biochemistry / FEBS
Volume:
232
Issue:
2
Pages:
515-521
Publication date:
1995-09-05
DOI:
EISSN:
1432-1033
ISSN:
0014-2956
URN:
uuid:d4cf41ba-04f2-42f9-8b5c-a520c3943481
Source identifiers:
108521
Local pid:
pubs:108521

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