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1.
Microsc Microanal ; 25(3): 630-638, 2019 Jun.
Artigo em Inglês | MEDLINE | ID: mdl-30757980

RESUMO

Silver nanowire (AgNW) diameters are typically characterized by manual measurement from high magnification electron microscope images. Measurement is monotonous and has potential ergonomic hazards. Because of this, statistics regarding wire diameter distribution can be poor, costly, and low-throughput. In addition, manual measurements are of unknown uncertainty and operator bias. In this paper we report an improved microscopy method for diameter and yield measurement of nanowires in terms of speed/automation and reduction of analyst variability. Each step in the process to generate these measurements was analyzed and optimized: microscope imaging conditions, sample preparation for imaging, image acquisition, image analysis, and data processing. With the resulting method, average diameter differences between samples of just a few nanometers can be confidently and statistically distinguished, allowing the identification of subtle incremental improvements in reactor processing conditions, and insight into nucleation and growth kinetics of AgNWs.

2.
Biomacromolecules ; 11(10): 2539-44, 2010 Oct 11.
Artigo em Inglês | MEDLINE | ID: mdl-20831150

RESUMO

The formation of calcite prism architecture in the prismatic layer of the mollusk shell involves the participation of a number of different proteins. One protein family, Asprich, has been identified as a participant in amorphous calcium carbonate stabilization and calcite architecture in the prismatic layer of the mollusk, Atrina rigida . However, the functional role(s) of this protein family are not fully understood due to the fact that insufficient quantities of these proteins are available for experimentation. To overcome this problem, we employed stepwise solid-phase synthesis to recreate one of the 10 members of the Asprich family, the 61 AA single chain protein, Asprich "3". We find that the Asprich "3" protein inhibits the formation of rhombohedral calcite crystals and induces the formation of round calcium carbonate deposits in vitro that contain calcite and amorphous calcium carbonate (ACC). This mineralization behavior does not occur under control conditions, and the formation of ACC and calcite is similar to that reported for the recombinant form of the Asprich "g" protein. Circular dichroism studies reveal that Asprich "3" is an intrinsically disordered protein, predominantly random coil (66%), with 20-30% ß-strand content, a small percentage of ß-turn, and little if any α-helical content. This protein is not extrinsically stabilized by Ca(II) ions but can be stabilized by 2,2,2-trifluoroethanol to form a structure consisting of turn-like and random coil characteristics. This finding suggests that Asprich "3" may require other extrinsic interactions (i.e., with mineral or ionic clusters or other macromolecules) to achieve folding. In conclusion, Asprich "3" possesses in vitro functional and structural qualities that are similar to other reported for other Asprich protein sequences.


Assuntos
Bivalves/química , Carbonato de Cálcio/química , Proteínas/química , Sequência de Aminoácidos , Animais , Bivalves/metabolismo , Bivalves/ultraestrutura , Carbonato de Cálcio/metabolismo , Cromatografia Líquida de Alta Pressão , Dicroísmo Circular , Cristalização , Microscopia Eletrônica de Varredura , Dados de Sequência Molecular , Conformação Proteica , Dobramento de Proteína , Proteínas/metabolismo , Proteínas Recombinantes/química , Proteínas Recombinantes/metabolismo , Espectrometria de Massas por Ionização e Dessorção a Laser Assistida por Matriz , Difração de Raios X
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