dc.contributor.author
Hodošček, Milan
dc.contributor.author
Elghobashi-Meinhardt, Nadia
dc.date.accessioned
2019-01-07T11:47:32Z
dc.date.available
2019-01-07T11:47:32Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/23640
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-1426
dc.description.abstract
A combination of molecular dynamics (MD) simulations and computational analyses uncovers structural features that may influence substrate passage and exposure to the active sites within the proteolytic chamber of the 20S proteasome core particle (CP). MD simulations of the CP reveal relaxation dynamics in which the CP slowly contracts over the 54 ns sampling period. MD simulations of the SyringolinA (SylA) inhibitor within the proteolytic B1 ring chamber of the CP indicate that favorable van der Waals and electrostatic interactions account for the predominant association of the inhibitor with the walls of the proteolytic chamber. The time scale required for the inhibitor to travel from the center of the proteolytic chamber to the chamber wall is on the order of 4 ns, accompanied by an average energetic stabilization of approximately −20 kcal/mol.
en
dc.format.extent
18 Seiten
dc.rights.uri
https://creativecommons.org/licenses/by/4.0/
dc.subject
core particle (CP)
en
dc.subject
SyringolinA inhibitor
en
dc.subject
molecular dynamics (MD)
en
dc.subject
electrostatic interactions
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::570 Biowissenschaften; Biologie::572 Biochemie
dc.title
Insight into Inhibitor Binding in the Eukaryotic Proteasome: Computations of the 20S CP
dc.type
Wissenschaftlicher Artikel
dc.date.updated
2018-12-21T14:51:47Z
dcterms.bibliographicCitation.articlenumber
3858
dcterms.bibliographicCitation.doi
10.3390/ijms19123858
dcterms.bibliographicCitation.journaltitle
International Journal of Molecular Sciences
dcterms.bibliographicCitation.number
12
dcterms.bibliographicCitation.volume
19
refubium.affiliation
Biologie, Chemie, Pharmazie
refubium.affiliation.other
Institut für Chemie und Biochemie
refubium.funding
Institutional Participation
refubium.funding.id
MDPI
refubium.note.author
Die Publikation wurde aus Open Access Publikationsgeldern der Freien Universität Berlin und der DFG gefördert.
refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.issn
1661-6596
dcterms.isPartOf.issn
1422-0067