Aragonite-associated biomineralization proteins are disordered and contain interactive motifs
Author(s) -
John Spencer Evans
Publication year - 2012
Publication title -
bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.599
H-Index - 390
eISSN - 1367-4811
pISSN - 1367-4803
DOI - 10.1093/bioinformatics/bts604
Subject(s) - aragonite , biomineralization , protein sequencing , mineralized tissues , chemistry , biophysics , biology , protein structure , intrinsically disordered proteins , peptide sequence , crystallography , biochemistry , evolutionary biology , gene , materials science , mineralogy , calcite , paleontology , composite material , dentin
The formation of aragonite mineral in the mollusk shell or pearl nacre requires the participation of a diverse set of proteins that form the mineralized extracellular matrix. Although self-assembly processes have been identified for several nacre proteins, these proteins do not contain known globular protein-protein binding domains. Thus, we hypothesize that other sequence features are responsible for nacre matrix protein-protein assembly processes and ultimately aragonite biosynthesis.
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