Next Article in Journal
Schwertmannite Adherence to the Reactor Wall during the Bio-Synthesis Process and Deterioration of Its Structural Characteristics and Arsenic(III) Removal Efficiency
Next Article in Special Issue
Crystal Chemistry and Stability of Hydrated Rare-Earth Phosphates Formed at Room Temperature
Previous Article in Journal
Effect of the Structure of Alkyl Salicylaldoxime on Extraction of Copper(II)
Previous Article in Special Issue
In Situ AFM Study of Crystal Growth on a Barite (001) Surface in BaSO4 Solutions at 30 °C
Article Menu
Issue 4 (April) cover image

Export Article

Open AccessCommentary
Minerals 2017, 7(4), 62; https://doi.org/10.3390/min7040062

Polymorphs, Proteins, and Nucleation Theory: A Critical Analysis

Department of Basic Sciences, Skeletal Biology and Craniofacial Medicine, New York University, 345 E. 24th Street, New York, NY 10010, USA
Academic Editor: Denis Gebauer
Received: 1 April 2017 / Revised: 15 April 2017 / Accepted: 18 April 2017 / Published: 21 April 2017
Full-Text   |   PDF [1908 KB, uploaded 21 April 2017]   |  

Abstract

Over the last eight years new theories regarding nucleation, crystal growth, and polymorphism have emerged. Many of these theories were developed in response to observations in nature, where classical nucleation theory failed to account for amorphous mineral precursors, phases, and particle assembly processes that are responsible for the formation of invertebrate mineralized skeletal elements, such as the mollusk shell nacre layer (aragonite polymorph) and the sea urchin spicule (calcite polymorph). Here, we summarize these existing nucleation theories and place them within the context of what we know about biomineralization proteins, which are likely participants in the management of mineral precursor formation, stabilization, and assembly into polymorphs. With few exceptions, much of the protein literature confirms that polymorph-specific proteins, such as those from mollusk shell nacre aragonite, can promote polymorph formation. However, past studies fail to provide important mechanistic insights into this process, owing to variations in techniques, methodologies, and the lack of standardization in mineral assay experimentation. We propose that the way forward past this roadblock is for the protein community to adopt standardized nucleation assays and approaches that are compatible with current and emerging nucleation precursor studies. This will allow cross-comparisons, kinetic observations, and hopefully provide the information that will explain how proteins manage polymorph formation and stabilization. View Full-Text
Keywords: polymorphs; sea urchin; mollusk; calcite; vaterite; aragonite; biomineralization; proteins; classical nucleation theory; crystallization by particle attachment; non-classical nucleation polymorphs; sea urchin; mollusk; calcite; vaterite; aragonite; biomineralization; proteins; classical nucleation theory; crystallization by particle attachment; non-classical nucleation
Figures

Graphical abstract

This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
SciFeed

Share & Cite This Article

MDPI and ACS Style

Evans, J.S. Polymorphs, Proteins, and Nucleation Theory: A Critical Analysis. Minerals 2017, 7, 62.

Show more citation formats Show less citations formats

Note that from the first issue of 2016, MDPI journals use article numbers instead of page numbers. See further details here.

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Minerals EISSN 2075-163X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top