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© 1993 SAGE Publications Structural Characteristics of Human Salivary Statherin: A Model for Boundary Lubrication at the Enamel SurfaceDepartment of Oral Biology, Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, NY 14214
Department of Oral Biology, Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, NY 14214, Also at Department of Biophysics, Roswell Park Cancer Institute, Elm Street, Buffalo NY 14263
Department of Oral Biology, Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, NY 14214
Department of Oral Biology, Dental Research Institute, School of Dental Medicine, State University of New York at Buffalo, Buffalo, NY 14214 A three-dimensional structural model for salivary statherin in aqueous phase has been developed using structure prediction, circular dichroism, molecular modeling, and mechanics. The relevant structural features of statherin are N-terminal helix segment connected to a long poly-L-proline type II segment, which is followed by a short extended structure. Using this model, the hydroxyapatite binding ability of statherin has been explained. The hydroxyapatite binding region is comprised of the N-terminal acidic residues (Asp-pSer-pSer-Glu-Glu) and Glu-26, which are clustered together in space. Partial conformational unfolding and oriented aggregation of several statherin molecules at the enamel surface provides an amphipathic film that is responsible for the boundary lubrication exhibited by statherin.
Key Words: statherin molecular modeling circular dichroism lubrication conformational unfolding.
Critical Reviews in Oral Biology & Medicine, Vol. 4, No. 3,
363-370 (1993) This article has been cited by other articles:
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