Influence of the Temperature on the Proton Transport in Poly(styrene-co-divinylbenzene) Membranes from Molecular Dynamics Simulations

2014 ◽  
Vol 118 (31) ◽  
pp. 17643-17654 ◽  
Author(s):  
Esther Córdova-Mateo ◽  
Oscar Bertran ◽  
Carlos Alemán
Keyword(s):  
Molecular Dynamics ◽  
Molecular Dynamics Simulations ◽  
Proton Transport ◽  
Dynamics Simulations

Proton transport mechanism of imidazole, triazole and phosphoric acid mixtures from ab initio molecular dynamics simulations

2015 ◽  
Vol 17 (45) ◽  
pp. 30551-30559 ◽  
Author(s):  
Swagata Pahari ◽  
Sudip Roy
Keyword(s):  
Molecular Dynamics ◽  
Phosphoric Acid ◽  
Ab Initio ◽  
Molecular Dynamics Simulations ◽  
First Principles ◽  
Proton Transport ◽  
Transport Mechanism ◽  
Ab Initio Molecular Dynamics ◽  
Dynamics Simulations

We have performed first principles molecular dynamics simulations to elucidate the mechanism and role of 1,2,3-triazole in proton transport while it is mixed with phosphoric acid (PA) and a phosphoric acid imidazole mixture.

scholarly journals Protonation Dynamics in the K-Channel of Cytochrome c Oxidase Estimated from Molecular Dynamics Simulations

Processes ◽  
2021 ◽  
Vol 9 (2) ◽  
pp. 265
Author(s):  
Vincent Stegmaier ◽  
Rene F. Gorriz ◽  
Petra Imhof
Keyword(s):  
Molecular Dynamics ◽  
Cytochrome C ◽  
Proton Transfer ◽  
Molecular Dynamics Simulations ◽  
Cytochrome C Oxidase ◽  
Proton Transport ◽  
K Channel ◽  
Proton Transfer Reactions ◽  
Dynamics Simulations ◽  
Hydrogen Bonded

Proton transfer reactions are one of the most fundamental processes in biochemistry. We present a simplistic approach for estimating proton transfer probabilities in a membrane protein, cytochrome c oxidase. We combine short molecular dynamics simulations at discrete protonation states with a Monte Carlo approach to exchange between those states. Requesting for a proton transfer the existence of a hydrogen-bonded connection between the two source and target residues of the exchange, restricts the acceptance of transfers to only those in which a proton-relay is possible. Together with an analysis of the hydrogen-bonded connectivity in one of the proton-conducting channels of cytochrome c oxidase, this approach gives insight into the protonation dynamics of the hydrogen-bonded networks. The connectivity and directionality of the networks are coupled to the conformation of an important protein residue in the channel, K362, rendering proton transfer in the entire channel feasible in only one of the two major conformations. Proton transport in the channel can thus be regulated by K362 not only through its possible role as a proton carrier itself, but also by allowing or preventing proton transport via water residues.

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