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

被引：18

作者：

Buchko, Garry W. ^{[2
]}

Bekhazi, Jacky ^{[1
]}

Cort, John R. ^{[2
]}

Valentine, Nancy B. ^{[1
]}

Snead, Malcolm L. ^{[3
]}

Shaw, Wendy J. ^{[1
]}

机构：

[1] Pacific NW Natl Lab, Div Chem Sci, Richland, WA 99352 USA

[2] Pacific NW Natl Lab, Div Biol Sci, Richland, WA 99352 USA

[3] Univ So Calif, Ctr Craniofacial Mol Biol, Los Angeles, CA 90033 USA

来源：

BIOMOLECULAR NMR ASSIGNMENTS | 2008年 / 2卷 / 01期

关键词：

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

D O I：

10.1007/s12104-008-9092-x

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

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.

引用

页码：89 / 91

页数：3

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