Interruption of Hydrogen Bonding Networks of Water in Carbon Nanotubes Due to Strong Hydration Shell Formation

Langmuir ◽  
2017 ◽  
Vol 33 (42) ◽  
pp. 11120-11125 ◽  
Author(s):  
Yoshifumi Oya ◽  
Kenji Hata ◽  
Tomonori Ohba
2018 ◽  
Vol 54 (31) ◽  
pp. 3823-3826 ◽  
Author(s):  
Yusuke Nakanishi ◽  
Haruka Omachi ◽  
Natalie A. Fokina ◽  
Peter R. Schreiner ◽  
Jonathan Becker ◽  
...  

1,6-Bis(hydroxymethyl)diamantane forms one-dimensional networks inside carbon nanotubes through hydrogen bonding that leads to higher filling-yield as compared with pristine diamantane.


2020 ◽  
Vol 537 ◽  
pp. 110849
Author(s):  
Débora N. de Freitas ◽  
Bruno H.S. Mendonça ◽  
Mateus H. Köhler ◽  
Marcia C. Barbosa ◽  
Matheus J.S. Matos ◽  
...  

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

Small ◽  
2018 ◽  
Vol 14 (38) ◽  
pp. 1802307 ◽  
Author(s):  
Joanna Boucard ◽  
Camille Linot ◽  
Thibaut Blondy ◽  
Steven Nedellec ◽  
Philippe Hulin ◽  
...  

CrystEngComm ◽  
2016 ◽  
Vol 18 (1) ◽  
pp. 62-67
Author(s):  
Yoona Jang ◽  
Seo Yeon Yoo ◽  
Hye Rin Gu ◽  
Yu Jin Lee ◽  
Young Shin Cha ◽  
...  

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.


2016 ◽  
Vol 72 (1) ◽  
pp. 28-34
Author(s):  
Christian Neis ◽  
Bernd Morgenstern ◽  
Kaspar Hegetschweiler

A first preliminary report on the crystal structure of a hydrated salt formulated as [Ge(taci)2]Cl4·13H2O (taci is 1,3,5-triamino-1,3,5-trideoxy-cis-inositol) appeared more than 20 years ago [Ghisletta (1994). PhD thesis, ETH Zürich. Switzerland]. At that time it was not possible to discriminate unambiguously between the positions of some of the chloride ions and water O atoms, and disorder was thus postulated. In a new determination, a conclusive scheme of hydrogen bonding proves to be a particularly appealing aspect of the structure. Single crystals of the title compound, C12H30GeN6O64+·4Cl−·6H2O or [Ge(taci)2]2Cl8·12H2O, were grown from an aqueous solution by slow evaporation of the solvent. The two [Ge(taci)2]4+cations exhibit a double-adamantane-type structure with exclusive O-atom coordination and approximateD3dsymmetry. The taci ligands adopt a zwitterionic form with deprotonated hydroxy groups and protonated amino groups. Both cations are hydrogen bonded to six water molecules. The structure of the hydration shell of the two cations is, however, slightly different. The {[Ge(taci)2]·6H2O}4+aggregates are interlinked in all three dimensions by further hydrogen bonds of the types N—H...Cl...H—N, N—H...O(H)2...H—N, (Ge)O...H—O(H)...H—N, N—H...O(H)—H...Cl...H—N, (Ge)O...H—O—H...Cl...H—N, N—H...O(H)—H...Cl...H—(H)O...H—N, (Ge)O...H—O—H...Cl...H—(H)O...H—N and Ge(O)...H—O—H...Cl...H—O—H...O(Ge).


Biomolecules ◽  
2021 ◽  
Vol 11 (12) ◽  
pp. 1882
Author(s):  
Wei Xia ◽  
Yingguo Bai ◽  
Pengjun Shi

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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