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Default A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.

A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.

Related Articles A REDOR NMR study of a phosphorylated statherin fragment bound to hydroxyapatite crystals.

J Am Chem Soc. 2005 Jul 6;127(26):9350-1

Authors: Gibson JM, Raghunathan V, Popham JM, Stayton PS, Drobny GP

Hydroxyapatite (HAP) is the main mineral component of teeth. It is well-known that several salivary proteins and peptides bind strongly to HAP to regulate crystal growth. Interactions between a peptide derived from the N-terminal fragment of the salivary protein statherin and HAP were measured utilizing rotational-echo double-resonance (REDOR) nuclear magnetic resonance (NMR). The REDOR measurement from the side chain of the salivary peptide to the HAP surface is complicated by two effects: a possible additional dipolar coupling to a phosphorylated side chain and the potential proximity of phosphorus atoms to each other, resulting in a homonuclear dipolar interaction. Both of these effects were addressed, and the smallest model applicable to our system includes the nitrogen-15 (15N) spin in the lysine side chain and two phosphorus-31 (31P) spins, at least one of which must be from the surface phosphates of the HAP.

PMID: 15984845 [PubMed - indexed for MEDLINE]



Source: PubMed
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