Developing enamel matrix proteins: a conformation study of enamelins and amelogenins

Autor:	D. Perl-Treves, J.D. Termine, A. Jodaikin, Steve Weiner, Wolfie Traub
Rok vydání:	1987
Předmět:	Diffraction In situ Chemistry Infrared spectroscopy General Medicine Biochemistry Crystallography stomatognathic system Structural Biology X-ray crystallography Fourier transform infrared spectroscopy Amelogenin Enamel matrix proteins Molecular Biology Biomineralization
Zdroj:	International Journal of Biological Macromolecules. 9:166-168
ISSN:	0141-8130
DOI:	10.1016/0141-8130(87)90046-8
Popis:	Conformations of the organic matrix proteins in rat and bovine enamel were examined using X-ray diffraction and fourier transform infrared spectroscopy. These were compared with the extracted and purified proteins. The acidic enamelins, both in situ and in the purified form, are in the β-sheet conformation. The hydrophobic amelogenins, on the other hand, do not show any identifiable regular conformations in situ or when purified.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_________::0428d45acbb7e342f5a4f3d22710c2c8 https://doi.org/10.1016/0141-8130(87)90046-8 Zobrazit plný text záznamu