dc.contributor.author
Bondar, Ana-Nicoleta
dc.date.accessioned
2021-06-17T11:22:20Z
dc.date.available
2021-06-17T11:22:20Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/31059
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-30795
dc.description.abstract
Membrane-bound proteins that change protonation during function use specific protein groups to bind and transfer protons. Knowledge of the identity of the proton-binding groups is of paramount importance to decipher the reaction mechanism of the protein, and protonation states of prominent are studied extensively using experimental and computational approaches. Analyses of model transporters and receptors from different organisms, and with widely different biological functions, indicate common structure-sequence motifs at internal proton-binding sites. Proton-binding dynamic hydrogen-bond networks that are exposed to the bulk might provide alternative proton-binding sites and proton-binding pathways. In this perspective article I discuss protonation coupling and proton binding at internal and external carboxylate sites of proteins that use proton transfer for function. An inter-helical carboxylate-hydroxyl hydrogen-bond motif is present at functionally important sites of membrane proteins from archaea to the brain. External carboxylate-containing H-bond clusters are observed at putative proton-binding sites of protonation-coupled model proteins, raising the question of similar functionality in spike protein S.
en
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
hydrogen-bonding
en
dc.subject
proton transfer
en
dc.subject
proton antenna
en
dc.subject
membrane transporter
en
dc.subject
spike protein S
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::530 Physik::530 Physik
dc.title
Proton-Binding Motifs of Membrane-Bound Proteins
dc.type
Wissenschaftlicher Artikel
dc.title.subtitle
From Bacteriorhodopsin to Spike Protein S
dcterms.bibliographicCitation.articlenumber
685761
dcterms.bibliographicCitation.doi
10.3389/fchem.2021.685761
dcterms.bibliographicCitation.journaltitle
Frontier in Chemistry
dcterms.bibliographicCitation.volume
9
dcterms.bibliographicCitation.url
https://doi.org/10.3389/fchem.2021.685761
refubium.affiliation
Physik
refubium.affiliation.other
Institut für Theoretische Physik
![This authority value has been confirmed as accurate by an interactive user](/cache_202e45ad85b55efaeb29160f63cd3f3b/themes/FuCD/images/authority_control/invisible.gif)
refubium.note.author
I acknowledge support from the Open Access Publication Initiative of the Freie Universität Berlin.
en
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access