scholarly journals Directed evolution of artificial repeat proteins as habit modifiers for the morphosynthesis of (111)-terminated gold nanocrystals

Nanoscale ◽  
2019 ◽  
Vol 11 (37) ◽  
pp. 17485-17497 ◽  
Author(s):  
Janak Prasad ◽  
Sébastien Viollet ◽  
Kargal L. Gurunatha ◽  
Agathe Urvoas ◽  
Agathe C. Fournier ◽  
...  

Artificial repeat proteins are selected by directed evolution for their high chemical affinity for gold and structural selectivity for (111) facets. The proteins chaperone the growth of (111)-terminated nanocrystals and form a functional shell.

1999 ◽  
Vol 564 ◽  
Author(s):  
Dong Kyun Sohn ◽  
Ji-Soo Park ◽  
Jong-Uk Bae ◽  
Yun-Jun Hub ◽  
Jin Won Park

AbstractWe studied reverse leakage current in n+/p titanium-salicided shallow junctions using C49 Ti-silicide as a diffusion source. After Ti deposition, rapid thermal annealing (RTA) was performed to form the C49 Ti-silicide. Subsequently, arsenic ions were implanted and a 2nd RTA was carried out at 850 °C to form the low resistivity C54 Ti-silicide. In spite of no drive-in process following the 2nd annealing, the implanted As diffused well into Si substrate and the reverse leakage current of the n+/p junctions was reduced to two orders of magnitude lower. Since the high chemical affinity of As to Ti-silicide trapped the dopant in the silicide, it has been known that Ti or Ti-silicide cannot be used as a diffusion source. However, in this work, we found that the C49 Ti-silicide acted as a diffusion source of As ions. The reason of fast diffusivity is attributed to the generation of high tensile stress induced by As implantation.


1882 ◽  
Vol 14 (347supp) ◽  
pp. 5538-5539
Author(s):  
Charles Morris
Keyword(s):  

1905 ◽  
Vol 60 (1547supp) ◽  
pp. 24792-24794 ◽  
Author(s):  
Oliver J. Lodge
Keyword(s):  

2019 ◽  
Author(s):  
Huifang Xu ◽  
Weinan Liang ◽  
Linlin Ning ◽  
Yuanyuan Jiang ◽  
Wenxia Yang ◽  
...  

P450 fatty acid decarboxylases (FADCs) have recently been attracting considerable attention owing to their one-step direct production of industrially important 1-alkenes from biologically abundant feedstock free fatty acids under mild conditions. However, attempts to improve the catalytic activity of FADCs have met with little success. Protein engineering has been limited to selected residues and small mutant libraries due to lack of an effective high-throughput screening (HTS) method. Here, we devise a catalase-deficient <i>Escherichia coli</i> host strain and report an HTS approach based on colorimetric detection of H<sub>2</sub>O<sub>2</sub>-consumption activity of FADCs. Directed evolution enabled by this method has led to effective identification for the first time of improved FADC variants for medium-chain 1-alkene production from both DNA shuffling and random mutagenesis libraries. Advantageously, this screening method can be extended to other enzymes that stoichiometrically utilize H<sub>2</sub>O<sub>2</sub> as co-substrate.


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