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Conformational and Dynamics Studies of Human Salivary Histatin Bound on Hydroxyapatite by Solid State NMR


EMSL Project ID
2166

Abstract

Biomineralization, a field that studies the formation of mineral tissues by organisms, offers structural biologists may opportunities to address some core issues of structure-function relationships and molecular recognition at interfaces. Some important implications of better understanding biomineralization include some new advances in materials science based on biomimetics. As part of our interest in biomineralization phenomena, we have been studying human salivary polypeptides found in the acquired enamel pellicle. In this proposal, we focus on histatin-5 a polypeptide which is histdine-rich, basice, and possesses at least two important functions: control of hydroxyaapatite (HAP) crystal growth and antimicrobial activity. Previous studies have characterized functionally important regions of the peptide sequence and some secondary conformation analysis in solution have been done.

Project Details

Project type
Capability Research
Start Date
2001-07-25
End Date
2001-08-07
Status
Closed

Team

Principal Investigator

Gary Drobny
Institution
University of Washington

Team Members

Myriam Cotten
Institution
Hamilton College