Role of Long-Range Electrostatic Interactions and Local Topology of the Hydrogen Bond Network in the Wettability of Fully and Partially Wetted Single and Multilayer Graphene

2021 ◽  
Vol 125 (11) ◽  
pp. 6367-6377
Author(s):  
Mara Chiricotto ◽  
Fausto Martelli ◽  
Giuliana Giunta ◽  
Paola Carbone
Keyword(s):  
Hydrogen Bond ◽  
Long Range ◽  
Electrostatic Interactions ◽  
Multilayer Graphene ◽  
Hydrogen Bond Network ◽  
Bond Network ◽  
Local Topology

ЭЛЕКТРОСТАТИЧЕСКОЕ ВЗАИМОДЕЙСТВИЕ ГЛОБИНОВ С ФОСФОЛИПИДНЫМИ МЕМБРАНАМИ

2020 ◽  
Vol 65 (6) ◽  
pp. 1072-1080
Author(s):  
Г.Б. Постникова ◽  
◽  
Е.А. Шеховцова ◽  
В.С. Сивожелезов ◽  
◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Electrostatic Interactions ◽  
Sperm Whale ◽  
Proximal Part ◽  
Hydrogen Bond Network ◽  
Protein Residues ◽  
Horse Heart Myoglobin ◽  
Bond Network ◽  
The Stability

The present study aimed to analyze the role of electrostatic interactions contributing to the stability of the native conformations of the heme group in the structure of sperm whale myoglobin (SWMb), horse heart myoglobin (HHMb), hemoglobin I (HbI) from the botfly Gasterophilus intestinalis (giHbI) and monomeric and dimeric hemoglobins HbI and HbII from the mollusk Lucina pectinata (lpHbI and lpHbII) as well as investigate a possible reason of destabilization due to interaction with negatively charged phospholipid membranes. It was shown that the native conformation of the heme cavity in these globins, both in its proximal and distal sides, is sustained by a system of hydrogen bonds involving the proximal and distal protein residues, both heme propionic acid groups and the nearby polar amino acids on the protein surface (His, Arg, Lys). The hydrogen bond network in the proximal part of the heme pocket controls the position of the Fe atom outside or in the protoporphyrin plane, affecting the efficiency of ligand binding, while in the distal part of the heme cavity the hydrogen bond network formed with the participation of the distal protein residue (HisE7 in swMb, hhMb and giHbI, and GlnE7 in lpHbII) should, apparently, stabilize conformation where the protein is able to donate hydrogen to O2 ligand...

The Role of a Conserved Internal Water Molecule and Its Associated Hydrogen Bond Network in Cytochrfome c

1994 ◽  
Vol 236 (3) ◽  
pp. 786-799 ◽  
Author(s):  
Albert M. Berghuis ◽  
J.Guy Guillemette ◽  
George McLendon ◽  
Fred Sherman ◽  
Michael Smith ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Water Molecule ◽  
Hydrogen Bond Network ◽  
Internal Water ◽  
Bond Network

scholarly journals Energetics of the Proton Transfer Pathway for Tyrosine D in Photosystem II

2016 ◽  
Vol 69 (9) ◽  
pp. 991 ◽  
Author(s):  
Keisuke Saito ◽  
Naoki Sakashita ◽  
Hiroshi Ishikita
Keyword(s):  
Hydrogen Bond ◽  
Photosystem Ii ◽  
Proton Transfer ◽  
Electrostatic Interactions ◽  
Water Molecules ◽  
Hydrogen Bond Network ◽  
Redox States ◽  
Redox Active ◽  
Bond Network ◽  
Tyrosine D

The proton transfer pathway for redox active tyrosine D (TyrD) in photosystem II is a hydrogen-bond network that involves D2-Arg180 and a series of water molecules. Using quantum mechanical/molecular mechanical calculations, the detailed properties of the energetics and structural geometries were investigated. The potential-energy profile of all hydrogen bonds along the proton transfer pathway indicates that the overall proton transfer from TyrD is energetically downhill. D2-Arg180 plays a key role in the proton transfer pathway, providing a driving force for proton transfer, maintaining the hydrogen-bond network structure, stabilising P680•+, and thus deprotonating TyrD-OH to TyrD-O•. A hydrophobic environment near TyrD enhances the electrostatic interactions between TyrD and redox active groups, e.g. P680 and the catalytic Mn4CaO5 cluster: the redox states of those groups are linked with the protonation state of TyrD, i.e. release of the proton from TyrD. Thus, the proton transfer pathway from TyrD may ultimately contribute to the conversion of S0 into S1 in the dark in order to stabilise the Mn4CaO5 cluster when the photocycle is interrupted in S0.

scholarly journals Engineering resistance to ‘aging’ of phosphylated human acetylcholinesterase Role of hydrogen bond network in the active center

FEBS Letters ◽  
1993 ◽  
Vol 334 (2) ◽  
pp. 215-220 ◽  
Author(s):  
Arie Ordentlich ◽  
Chanoch Kronman ◽  
Dov Barak ◽  
Dana Stein ◽  
Naomi Ariel ◽  
...  
Keyword(s):  
Hydrogen Bond ◽  
Active Center ◽  
Hydrogen Bond Network ◽  
Bond Network
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