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Controls of nature: Secondary, tertiary, and quaternary structure of the enamel protein amelogenin in solution and on hydroxyapatite.
Shaw, Wendy J; Tarasevich, Barbara J; Buchko, Garry W; Arachchige, Rajith M J; Burton, Sarah D.
Afiliação
  • Shaw WJ; Physical and Computational Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99352, USA. Electronic address: Wendy.shaw@pnnl.gov.
  • Tarasevich BJ; Physical and Computational Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
  • Buchko GW; Earth and Biological Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99352, USA; School of Molecular Bioscience, Washington State University, Pullman, WA 99164, USA.
  • Arachchige RMJ; Physical and Computational Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
  • Burton SD; Earth and Biological Sciences Directorate, Pacific Northwest National Laboratory, Richland, WA 99352, USA.
J Struct Biol ; 212(3): 107630, 2020 12 01.
Article em En | MEDLINE | ID: mdl-32979496
Amelogenin, a protein critical to enamel formation, is presented as a model for understanding how the structure of biomineralization proteins orchestrate biomineral formation. Amelogenin is the predominant biomineralization protein in the early stages of enamel formation and contributes to the controlled formation of hydroxyapatite (HAP) enamel crystals. The resulting enamel mineral is one of the hardest tissues in the human body and one of the hardest biominerals in nature. Structural studies have been hindered by the lack of techniques to evaluate surface adsorbed proteins and by amelogenin's disposition to self-assemble. Recent advancements in solution and solid state nuclear magnetic resonance (NMR) spectroscopy, atomic force microscopy (AFM), and recombinant isotope labeling strategies are now enabling detailed structural studies. These recent studies, coupled with insights from techniques such as CD and IR spectroscopy and computational methodologies, are contributing to important advancements in our structural understanding of amelogenesis. In this review we focus on recent advances in solution and solid state NMR spectroscopy and in situ AFM that reveal new insights into the secondary, tertiary, and quaternary structure of amelogenin by itself and in contact with HAP. These studies have increased our understanding of the interface between amelogenin and HAP and how amelogenin controls enamel formation.
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Texto completo: 1 Base de dados: MEDLINE Assunto principal: Durapatita / Proteínas do Esmalte Dentário / Amelogenina Idioma: En Ano de publicação: 2020 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Durapatita / Proteínas do Esmalte Dentário / Amelogenina Idioma: En Ano de publicação: 2020 Tipo de documento: Article