Chemistry Seminar Series: Harvey GoldbergExport this event to calendar

Wednesday, April 4, 2012 — 2:30 PM to 3:30 PM EDT

Structural-functional characteristics of the bone sialoprotein-mediated nucleation of hydroxyapaptite

Professor Harvey Goldberg
Department of Biochemistry
University of Western Ontario

Abstract:  Bone sialoprotein (BSP) is a highly acidic phosphorylated glycoprotein found at high levels in mineralized tissues. Similar to other members of the "SIBLING" protein family, BSP is a multidomain, multifunctional adhesive protein with a flexible conformation and little secondary structure. BSP has been demonstrated to be involved in cell attachment and signaling, hydroxyapatite binding and nucleation, and collagen binding. The flexible structure of BSP is believed critical in its ability to interact with multiple binding partners. Recent studies on the BSP-null mice have provided further evidence for a significant role for BSP in bone formation and remodeling.  However the true physiological relevance of the BSP sequences involved in hydroxyapatite binding and formation and the mechanism of how BSP promotes mineral formation remains to be determined.

Location 
C2 - Chemistry 2
Room 361
200 University Ave West

Waterloo, ON N2L 3G1
Canada

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