Kaleidoscopic Tiling Patterns with Large Unit Cells from ABC Star-Shaped Terpolymer/Diblock Copolymer Blends with Hydrogen Bonding Interaction

2017 ◽  
Vol 50 (3) ◽  
pp. 979-986 ◽  
Author(s):  
Haruko Miyase ◽  
Yusuke Asai ◽  
Atsushi Takano ◽  
Yushu Matsushita
2005 ◽  
Vol 38 (21) ◽  
pp. 8811-8815 ◽  
Author(s):  
Takeshi Asari ◽  
Shigeo Matsuo ◽  
Atsushi Takano ◽  
Yushu Matsushita

2019 ◽  
Vol E102.C (11) ◽  
pp. 813-817
Author(s):  
Yosei SHIBATA ◽  
Ryosuke SAITO ◽  
Takahiro ISHINABE ◽  
Hideo FUJIKAKE

2020 ◽  
Author(s):  
Hossein Khalilian ◽  
Gino A. DiLabio

Here, we report an exquisite strategy that the B12 enzymes exploit to manipulate the reactivity of their radical intermediate (Adenosyl radical). Based on the quantum-mechanic calculations, these enzymes utilize a little known long-ranged through space quantum Coulombic effect (QCE). The QCE causes the radical to acquire an electronic structure that contradicts the Aufbau Principle: The singly-occupied molecular orbital (SOMO) is no longer the highest-occupied molecular orbital (HOMO) and the radical is unable to react with neighbouring substrates. The dynamic nature of the enzyme and its structure is expected to be such that the reactivity of the radical is not restored until it is moved into close proximity of the target substrate. We found that the hydrogen bonding interaction between the nearby conserved glutamate residue and the ribose ring of Adenosyl radical plays a crucial role in manipulating the orbital ordering


2020 ◽  
Author(s):  
Hossein Khalilian ◽  
Gino A. DiLabio

Here, we report an exquisite strategy that the B12 enzymes exploit to manipulate the reactivity of their radical intermediate (Adenosyl radical). Based on the quantum-mechanic calculations, these enzymes utilize a little known long-ranged through space quantum Coulombic effect (QCE). The QCE causes the radical to acquire an electronic structure that contradicts the Aufbau Principle: The singly-occupied molecular orbital (SOMO) is no longer the highest-occupied molecular orbital (HOMO) and the radical is unable to react with neighbouring substrates. The dynamic nature of the enzyme and its structure is expected to be such that the reactivity of the radical is not restored until it is moved into close proximity of the target substrate. We found that the hydrogen bonding interaction between the nearby conserved glutamate residue and the ribose ring of Adenosyl radical plays a crucial role in manipulating the orbital ordering


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