|Title||Structural disorder in proteins brings order to crystal growth in biomineralization.|
|Publication Type||Journal Article|
|Year of Publication||2012|
|Authors||Kalmar, L., D. Homola, G. Varga, and P. Tompa|
|Date Published||2012 Sep|
|Type of Article||idp|
|Keywords||Amino Acids, Animals, Calcification, Physiologic, Crystallization, Humans, Protein Conformation, Proteins|
Biomineralization, the generation of hard tissues of living organisms, is a process strictly regulated by hormones, enzymes and a range of regulatory proteins of which several resisted structural characterization thus far. Without actual generalizations, there have been scattered observations in the literature for the structural disorder of these proteins. To address this issue in general, we have collected SwissProt proteins involved in the formation of bone and teeth in vertebrates, annotated for biomineralization. All these proteins show an extremely high level of predicted disorder (with a mean of 53%), making them the most disordered functional class of the protein world. Exactly the same feature was established for evolutionarily more distant proteins involved in the formation of the silica wall of marine diatoms and the shell of oysters and other mollusks. Because these proteins also show an extremely biased amino acid composition, such as high negative charge, high frequency of Ser and Asp or Pro residues and repetitiveness, we also carried out a database search with these sequence features for further proteins. This search uncovered several further disordered proteins with clearly related functions, although their annotations made no mention of biomineralization. This general and very strong correlation between biomineralization, structural disorder of proteins and particular sequence features indicates that regulated growth of mineral phase in biology can only be achieved by the assistance of highly disordered proteins.