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Proteins as strongly correlated protonic systems
Author(s) -
Couch Ver,
Stuchebrukhov Alexei
Publication year - 2012
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2011.09.036
Subject(s) - protonation , ergodicity , statistical physics , monte carlo method , chemistry , eigenvalues and eigenvectors , state (computer science) , chemical physics , molecular dynamics , computational chemistry , physics , mathematics , quantum mechanics , ion , statistics , algorithm , organic chemistry
Determination of the protonation state of enzymes is a challenging problem in computational biophysics largely due to the vast number of possible protonic configurations. The protonation state dynamics of respiratory complex I was investigated via Monte Carlo and asynchronous dynamics simulations and a novel eigenvector analysis. Many low lying states were identified and examined. The analysis revealed that the protonic states form a quasi‐continuous band of energies, which are highly correlated and inhomogeneous. Many states have similar energies, but differ significantly in their protonic composition. In order to transfer from one such state to another, a large number of protons should be exchanged simultaneously raising the question of the ergodicity of protonation dynamics of such systems.