4.0 Article

1H, 13C, and 15N resonance assignments of murine amelogenin, an enamel biomineralization protein

Journal

BIOMOLECULAR NMR ASSIGNMENTS
Volume 2, Issue 1, Pages 89-91

Publisher

SPRINGER
DOI: 10.1007/s12104-008-9092-x

Keywords

enamel; amelogenin; biomineralization; unfolded protein; polyproline type II structure

Funding

  1. NIH-NIDCR [DE-015347]

Ask authors/readers for more resources

Amelogenin is the predominant matrix protein in developing dental enamel. Making extensive use of residue-specific N-15-labeled amino acids samples, the majority of the main and side chain resonances for murine amelogenin were assigned in 2% aqueous acetic acid at pH 3.0.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.0
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available