Chinese Journal of Magnetic Resonance >
Conformation of the N-Terminal Fragment of Human Salivary Statherin
1. Department of Chemistry, Taiwan University, Taipei 106, China; 2. Genomics Research Center, Taipei 115, China
Received date: 2015-02-11
Revised date: 2015-05-13
Online published: 2015-06-05
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Human salivary statherin is a 43-residue acidic phosphoprotein present in human saliva, possessing a high affinity for calcium phosphate minerals such as hydroxyapatite. The N-terminal 15-residue fragment of statherin (SN-15) is known to bind strongly to the crystallites of hydroxyapatite. In this work, we investigate the conformation of SN-15 in aqueous solution by NMR. Analysis of the CD spectra shows that SN-15 adopts an α-helical structure in phosphate buffer. High-resolution proton NMR spectra (COSY, TOCSY, and NOESY) have been acquired, from which the NOE patterns and J-couplings of amide hydrogens have been obtained. Together with the constraints obtained from amide-hydrogen exchange experiments, the molecular structure of SN-15 has shown to be a continuous α-helical structure.
Key words： biomineralization; HAp; SN-15
GUO Syuan-ming1 , CHANG Chi-fon2 , CHAN Jerry C C1*? . Conformation of the N-Terminal Fragment of Human Salivary Statherin[J]. Chinese Journal of Magnetic Resonance, 2015 , 32(2) : 283 -290 . DOI: 10.11938/cjmr20150211
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