Quantum Theoretical Evidence for Two Distinct Hydrogen-Bonding Networks and for an Ising Chain Model of the Antiferroelectric Transition in Squaric Acid

2002 ◽  
Vol 106 (18) ◽  
pp. 4799-4805 ◽  
Author(s):  
J. Palomar ◽  
N. S. Dalal
Keyword(s):  
Hydrogen Bonding ◽  
Squaric Acid ◽  
Chain Model ◽  
Ising Chain ◽  
Hydrogen Bonding Networks ◽  
Theoretical Evidence

scholarly journals The Multiple Hydrogen-Bonding Networks of Polyol Ribitol

2018 ◽  
Vol 24 (51) ◽  
pp. 13408-13412 ◽  
Author(s):  
Isabel Peña ◽  
Maria Eugenia Sanz ◽  
Elena R. Alonso ◽  
José L. Alonso
Keyword(s):  
Hydrogen Bonding ◽  
Hydrogen Bonding Networks ◽  
Multiple Hydrogen Bonding

Small Molecule-Based Fluorescent Organic Nanoassemblies with Strong Hydrogen Bonding Networks for Fine Tuning and Monitoring Drug Delivery in Cancer Cells

Small ◽  
2018 ◽  
Vol 14 (38) ◽  
pp. 1802307 ◽  
Author(s):  
Joanna Boucard ◽  
Camille Linot ◽  
Thibaut Blondy ◽  
Steven Nedellec ◽  
Philippe Hulin ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Hydrogen Bonding ◽  
Cancer Cells ◽  
Small Molecule ◽  
Fine Tuning ◽  
Monitoring Drug ◽  
Hydrogen Bonding Networks

Hydrogen-bonding networks of purine derivatives and their bilayers for guest intercalation

CrystEngComm ◽  
2016 ◽  
Vol 18 (1) ◽  
pp. 62-67
Author(s):  
Yoona Jang ◽  
Seo Yeon Yoo ◽  
Hye Rin Gu ◽  
Yu Jin Lee ◽  
Young Shin Cha ◽  
...  
Keyword(s):  
Hydrogen Bonding ◽  
Two Dimensional ◽  
Purine Derivatives ◽  
Guest Molecules ◽  
Π Interactions ◽  
Hydrogen Bonding Networks ◽  
Hydrogen Bonded

6-Chloro-9-propyl-purin-2-amine (pr-GCl) forms two-dimensional hydrogen-bonded networks which in turn stack via π–π interactions, leading to the formation of bilayers that can accommodate organic guest molecules.

scholarly journals Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A from Talaromyces leycettanus JCM12802 by Rational Design

Biomolecules ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1882
Author(s):  
Wei Xia ◽  
Yingguo Bai ◽  
Pengjun Shi
Keyword(s):  
Hydrogen Bonding ◽  
Rational Design ◽  
Substrate Binding ◽  
Enzymatic Saccharification ◽  
Catalytic Efficiency ◽  
Binding Pocket ◽  
Glycoside Hydrolases ◽  
Cellulosic Biomass ◽  
Substrate Affinity ◽  
Hydrogen Bonding Networks

Improving the substrate affinity and catalytic efficiency of β-glucosidase is necessary for better performance in the enzymatic saccharification of cellulosic biomass because of its ability to prevent cellobiose inhibition on cellulases. Bgl3A from Talaromyces leycettanus JCM12802, identified in our previous work, was considered a suitable candidate enzyme for efficient cellulose saccharification with higher catalytic efficiency on the natural substrate cellobiose compared with other β-glucosidase but showed insufficient substrate affinity. In this work, hydrophobic stacking interaction and hydrogen-bonding networks in the active center of Bgl3A were analyzed and rationally designed to strengthen substrate binding. Three vital residues, Met36, Phe66, and Glu168, which were supposed to influence substrate binding by stabilizing adjacent binding site, were chosen for mutagenesis. The results indicated that strengthening the hydrophobic interaction between stacking aromatic residue and the substrate, and stabilizing the hydrogen-bonding networks in the binding pocket could contribute to the stabilized substrate combination. Four dominant mutants, M36E, M36N, F66Y, and E168Q with significantly lower Km values and 1.4–2.3-fold catalytic efficiencies, were obtained. These findings may provide a valuable reference for the design of other β-glucosidases and even glycoside hydrolases.

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