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@ARTICLE{Bondar:943340,
author = {Bondar, Ana-Nicoleta},
title = {{M}echanisms of long-distance allosteric couplings in
proton-binding membrane transporters},
journal = {Advances in protein chemistry and structural biology},
volume = {128},
issn = {1876-1623},
address = {Heidelberg},
publisher = {Elsevier},
reportid = {FZJ-2023-00946},
pages = {199-238},
year = {2022},
abstract = {Membrane transporters that use proton binding and proton
transfer for function couple local protonation change with
changes in protein conformation and water dynamics. Changes
of protein conformation might be required to allow transient
formation of hydrogen-bond networks that bridge proton donor
and acceptor pairs separated by long distances.
Inter-helical hydrogen-bond networks adjust rapidly to
protonation change, and ensure rapid response of the protein
structure and dynamics. Membrane transporters with known
three-dimensional structures and proton-binding groups
inform on general principles of protonation-coupled protein
conformational dynamics. Inter-helical hydrogen bond motifs
between proton-binding carboxylate groups and a polar
sidechain are observed in unrelated membrane transporters,
suggesting common principles of coupling protonation change
with protein conformational dynamics.},
cin = {IAS-5 / INM-9},
ddc = {540},
cid = {I:(DE-Juel1)IAS-5-20120330 / I:(DE-Juel1)INM-9-20140121},
pnm = {5241 - Molecular Information Processing in Cellular Systems
(POF4-524)},
pid = {G:(DE-HGF)POF4-5241},
typ = {PUB:(DE-HGF)16},
pubmed = {35034719},
UT = {WOS:000873703000006},
doi = {10.1016/bs.apcsb.2021.09.002},
url = {https://juser.fz-juelich.de/record/943340},
}