dc.contributor.author
Düttmann, Markus
dc.contributor.author
Mittnenzweig, Markus
dc.contributor.author
Togashi, Yuichi
dc.contributor.author
Yanagida, Toshio
dc.contributor.author
Mikhailov, Alexander S.
dc.date.accessioned
2018-06-08T04:13:54Z
dc.date.available
2015-11-23T10:50:42.391Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/16860
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-21041
dc.description.abstract
Systematic numerical investigations of conformational motions in single actin
molecules were performed by employing a simple elastic-network (EN) model of
this protein. Similar to previous investigations for myosin, we found that
G-actin essentially behaves as a strain sensor, responding by well-defined
domain motions to mechanical perturbations. Several sensitive residues within
the nucleotide-binding pocket (NBP) could be identified, such that the
perturbation of any of them can induce characteristic flattening of actin
molecules and closing of the cleft between their two mobile domains. Extending
the EN model by introduction of a set of breakable links which become
effective only when two domains approach one another, it was observed that
G-actin can possess a metastable state corresponding to a closed conformation
and that a transition to this state can be induced by appropriate
perturbations in the NBP region. The ligands were roughly modeled as a single
particle (ADP) or a dimer (ATP), which were placed inside the NBP and
connected by elastic links to the neighbors. Our approximate analysis suggests
that, when ATP is present, it stabilizes the closed conformation of actin.
This may play an important role in the explanation why, in the presence of
ATP, the polymerization process is highly accelerated.
en
dc.rights.uri
http://creativecommons.org/licenses/by/2.0/de/
dc.subject.ddc
500 Naturwissenschaften und Mathematik
dc.title
Complex Intramolecular Mechanics of G-actin - An Elastic Network Study
dc.type
Wissenschaftlicher Artikel
dcterms.bibliographicCitation
PLoS ONE. - 7 (2012), 10, Artikel Nr. e45859
dcterms.bibliographicCitation.doi
10.1371/journal.pone.0045859
dcterms.bibliographicCitation.url
http://journals.plos.org/plosone/article?id=10.1371/journal.pone.0045859
refubium.affiliation
Mathematik und Informatik
de
refubium.mycore.fudocsId
FUDOCS_document_000000023507
refubium.note.author
Der Artikel wurde in einer Open-Access-Zeitschrift publiziert.
refubium.resourceType.isindependentpub
no
refubium.mycore.derivateId
FUDOCS_derivate_000000005695
dcterms.accessRights.openaire
open access