Optimizing GaxOy Growth Tendency of 3D Structures on Different Substrates through the MOCVD Technique

2019 ◽  
Vol 8 (7) ◽  
pp. Q3254-Q3258
Author(s):  
Maria Yaseen ◽  
Frederico D. Nunes ◽  
Marco Sacciloti ◽  
Emery C. Lins
Keyword(s):  
3D Structures ◽  
Mocvd Technique

From Levinthal’s Paradox to the Effects of Cell Environmental Perturbation on Protein Folding

2020 ◽  
Vol 26 (42) ◽  
pp. 7537-7554 ◽  
Author(s):  
Juan Zeng ◽  
Zunnan Huang
Keyword(s):  
Protein Folding ◽  
Posttranslational Modifications ◽  
Three Dimensional ◽  
Rational Drug Design ◽  
Basic Knowledge ◽  
Sequence Evolution ◽  
3D Structures ◽  
Folding Mechanism ◽  
Cellular Environment ◽  
Environment Temperature

Background: The rapidly increasing number of known protein sequences calls for more efficient methods to predict the Three-Dimensional (3D) structures of proteins, thus providing basic knowledge for rational drug design. Understanding the folding mechanism of proteins is valuable for predicting their 3D structures and for designing proteins with new functions and medicinal applications. Levinthal’s paradox is that although the astronomical number of conformations possible even for proteins as small as 100 residues cannot be fully sampled, proteins in nature normally fold into the native state within timescales ranging from microseconds to hours. These conflicting results reveal that there are factors in organisms that can assist in protein folding. Methods: In this paper, we selected a crowded cell-like environment and temperature, and the top three Posttranslational Modifications (PTMs) as examples to show that Levinthal’s paradox does not reflect the folding mechanism of proteins. We then revealed the effects of these factors on protein folding. Results: The results summarized in this review indicate that a crowded cell-like environment, temperature, and the top three PTMs reshape the Free Energy Landscapes (FELs) of proteins, thereby regulating the folding process. The balance between entropy and enthalpy is the key to understanding the effect of the crowded cell-like environment and PTMs on protein folding. In addition, the stability/flexibility of proteins is regulated by temperature. Conclusion: This paper concludes that the cellular environment could directly intervene in protein folding. The long-term interactions of the cellular environment and sequence evolution may enable proteins to fold efficiently. Therefore, to correctly understand the folding mechanism of proteins, the effect of the cellular environment on protein folding should be considered.

Novel additively manufactured bio-inspired 3D structures for impact energy damping

CIRP Annals ◽  
2021 ◽  
Author(s):  
Georgios Maliaris ◽  
Apostolos Argyros ◽  
Emmanouil Smyrnaios ◽  
Nikolaos Michailidis
Keyword(s):  
Impact Energy ◽  
3D Structures

scholarly journals Quantitative analysis of 3D structures in metal-oxide composites

2021 ◽  
Vol 27 (S1) ◽  
pp. 2974-2975
Author(s):  
Yu Wen ◽  
Ayako Hashimoto ◽  
Akihiko Hirata ◽  
Hideki Abe
Keyword(s):  
Quantitative Analysis ◽  
Metal Oxide ◽  
3D Structures ◽  
Oxide Composites

scholarly journals Refractive index matched polymeric and preceramic resins for height-scalable two-photon lithography

RSC Advances ◽  
2021 ◽  
Vol 11 (37) ◽  
pp. 22633-22639
Author(s):  
Magi Mettry ◽  
Matthew A. Worthington ◽  
Brian Au ◽  
Jean-Baptiste Forien ◽  
Swetha Chandrasekaran ◽  
...  
Keyword(s):  
Refractive Index ◽  
3D Structures ◽  
Two Photon

Studying the effect of resin RI on print fidelity. Chemically modifying RI resins to demonstrate 3D structures print without height limitation resulting on ceramic and nonceramic print as tall as 2.5 mm with sub-micron features.

scholarly journals Programmable shape-shifting 3D structures via frontal photopolymerization

2021 ◽  
Vol 198 ◽  
pp. 109381
Author(s):  
Jinqiang Wang ◽  
Ning Dai ◽  
Chengru Jiang ◽  
Xiaoming Mu ◽  
Biao Zhang ◽  
...  
Keyword(s):  
3D Structures
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