The role of nonbond and charge flux in hydrogen bond interactions. The effect on structural changes and spectral shifts in water dimer

1992 ◽  
Vol 97 (12) ◽  
pp. 9161-9172 ◽  
Author(s):  
U. Dinur ◽  
A. T. Hagler
Keyword(s):  
Hydrogen Bond ◽  
Structural Changes ◽  
Water Dimer ◽  
Hydrogen Bond Interactions ◽  
Spectral Shifts ◽  
Charge Flux

scholarly journals The synthesis of a pyridine-N-oxide isophthalamide rotaxane utilizing supplementary amide hydrogen bond interactions

2016 ◽  
Vol 14 (33) ◽  
pp. 7972-7981 ◽  
Author(s):  
Nicholas H. Evans ◽  
Charles E. Gell ◽  
Michael J. G. Peach
Keyword(s):  
Hydrogen Bond ◽  
Nmr Spectroscopy ◽  
Computational Modelling ◽  
Amide Hydrogen ◽  
X Ray ◽  
X Ray Crystallography ◽  
Hydrogen Bond Interactions

A pyridine-N-oxide containing rotaxane has been prepared in 32% yield. The role of macrocycle structure in successful pseudo-rotaxane formation has been rationalised by a combination of NMR spectroscopy, X-ray crystallography and computational modelling.

A theoretical study of the role of the hydrogen bond on core ionization of the water dimer

2005 ◽  
Vol 312 (1-3) ◽  
pp. 311-318 ◽  
Author(s):  
V.C. Felicı́ssimo ◽  
I. Minkov ◽  
F.F. Guimarães ◽  
F. Gel’mukhanov ◽  
A. Cesar ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Theoretical Study ◽  
Water Dimer

scholarly journals Supramolecular polymerisation in water; elucidating the role of hydrophobic and hydrogen-bond interactions

Soft Matter ◽  
2016 ◽  
Vol 12 (11) ◽  
pp. 2887-2893 ◽  
Author(s):  
Christianus M. A. Leenders ◽  
Matthew B. Baker ◽  
Imke A. B. Pijpers ◽  
René P. M. Lafleur ◽  
Lorenzo Albertazzi ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Self Assembly ◽  
The Self ◽  
Hydrogen Bond Interactions

The self-assembly of a family of benzene-1,3,5-tricarboxamides (BTAs) in water is studied systematically to elucidate the role of hydrophobic and hydrogen-bond interactions.

scholarly journals X-Ray Crystallographic Structure of the Norwalk Virus Protease at 1.5-Å Resolution

2006 ◽  
Vol 80 (10) ◽  
pp. 5050-5058 ◽  
Author(s):  
Corinne E. Zeitler ◽  
Mary K. Estes ◽  
B. V. Venkataram Prasad
Keyword(s):  
Hydrogen Bond ◽  
Conformational Changes ◽  
Cysteine Proteases ◽  
Catalytic Triad ◽  
Strong Hydrogen Bond ◽  
Crystallographic Structure ◽  
Viral Gastroenteritis ◽  
Norwalk Virus ◽  
Hydrogen Bond Interactions

ABSTRACT Norwalk virus (NV), a member of the Caliciviridae family, is the major cause of acute, epidemic, viral gastroenteritis. The NV genome is a positive sense, single-stranded RNA that encodes three open reading frames (ORFs). The first ORF produces a polyprotein that is processed by the viral cysteine protease into six nonstructural proteins. We have determined the structure of the NV protease to 1.5 and 2.2 Å from crystals grown in the absence or presence, respectively, of the protease inhibitor AEBSF [4-(2-aminoethyl)-benzenesulfonyl fluoride]. The protease, which crystallizes as a stable dimer, exhibits a two-domain structure similar to those of other viral cysteine proteases with a catalytic triad composed of His 30, Glu 54, and Cys 139. The native structure of the protease reveals strong hydrogen bond interactions between His 30 and Glu 54, in the favorable syn configuration, indicating a role of Glu 54 during proteolysis. Mutation of this residue to Ala abolished the protease activity, in a fluorogenic peptide substrate assay, further substantiating the role of Glu 54 during proteolysis. These observations contrast with the suggestion, from a previous study of another norovirus protease, that this residue may not have a prominent role in proteolysis (K. Nakamura, Y. Someya, T. Kumasaka, G. Ueno, M. Yamamoto, T. Sato, N. Takeda, T. Miyamura, and N. Tanaka, J. Virol. 79:13685-13693, 2005). In the structure from crystals grown in the presence of AEBSF, Glu 54 undergoes a conformational change leading to disruption of the hydrogen bond interactions with His 30. Since AEBSF was not apparent in the electron density map, it is possible that these conformational changes are due to subtle changes in pH caused by its addition during crystallization.

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