TY - JOUR
AU - Bondar, Ana-Nicoleta
TI - Mechanisms of long-distance allosteric couplings in proton-binding membrane transporters
JO - Advances in protein chemistry and structural biology
VL - 128
SN - 1876-1623
CY - Heidelberg
PB - Elsevier
M1 - FZJ-2023-00946
SP - 199-238
PY - 2022
AB - 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.
LB - PUB:(DE-HGF)16
C6 - 35034719
UR - <Go to ISI:>//WOS:000873703000006
DO - DOI:10.1016/bs.apcsb.2021.09.002
UR - https://juser.fz-juelich.de/record/943340
ER -