Proteins interact with biomineral surfaces to control crystal growth and final structure in biological systems ranging from seashell formation to teeth and bone. The elucidation of molecular recognition mechanisms at the organic-inorganic interface could provide inspiration for materials synthesis strategies. Solid state NMR (SSNMR) has been shown to be a powerful tool for determining the secondary structure of surface adsorbed proteins and can potentially provide important information on peptide dynamics at surfaces as a function of hydration.
Revised: May 2, 2001 |
Published: July 19, 2000
Citation
Shaw W.J., J.R. Long, A.A. Campbell, P.S. Stayton, P.S. Stayton, and G.P. Drobny. 2000.A Solid State NMR Study of Dynamics in a Hydrated Salivary Peptide Adsorbed to Hydroxyapatite.Journal of the American Chemical Society 122, no. 29:7118-7119. PNWD-SA-5109.