dc.contributor.author
Schwarzl, Richard
dc.contributor.author
Liese, Susanne
dc.contributor.author
Brünig, Florian N.
dc.contributor.author
Laudisio, Fabio
dc.contributor.author
Netz, Roland R.
dc.date.accessioned
2021-04-28T10:11:48Z
dc.date.available
2021-04-28T10:11:48Z
dc.identifier.uri
https://refubium.fu-berlin.de/handle/fub188/30181
dc.identifier.uri
http://dx.doi.org/10.17169/refubium-29922
dc.description.abstract
Using molecular dynamics simulations in explicit water, the force–extension relations for the five homopeptides polyglycine, polyalanine, polyasparagine, poly(glutamic acid), and polylysine are investigated. From simulations in the low-force regime the Kuhn length is determined, from simulations in the high-force regime the equilibrium contour length and the linear and nonlinear stretching moduli, which agree well with quantum-chemical density-functional theory calculations, are determined. All these parameters vary considerably between the different polypeptides. The augmented inhomogeneous partially freely rotating chain (iPFRC) model, which accounts for side-chain interactions and restricted dihedral rotation, is demonstrated to describe the simulated force–extension relations very well. We present a quantitative comparison between published experimental single-molecule force–extension curves for different polypeptides with simulation and model predictions. The thermodynamic stretching properties of polypeptides are investigated by decomposition of the stretching free energy into energetic and entropic contributions.
en
dc.format.extent
32 Seiten (Manuskriptversion)
dc.rights.uri
http://www.fu-berlin.de/sites/refubium/rechtliches/Nutzungsbedingungen
dc.subject
Peptides and proteins
en
dc.subject.ddc
500 Naturwissenschaften und Mathematik::530 Physik::530 Physik
dc.title
Force Response of Polypeptide Chains from Water-Explicit MD Simulations
dc.type
Wissenschaftlicher Artikel
dc.identifier.sepid
80461
dcterms.bibliographicCitation.doi
10.1021/acs.macromol.0c00138
dcterms.bibliographicCitation.journaltitle
Macromolecules
dcterms.bibliographicCitation.number
12
dcterms.bibliographicCitation.originalpublishername
American Chemical Society
dcterms.bibliographicCitation.originalpublisherplace
Washington, DC
dcterms.bibliographicCitation.pagestart
4618
dcterms.bibliographicCitation.pageend
4629
dcterms.bibliographicCitation.volume
53
dcterms.bibliographicCitation.url
https://pubs.acs.org/doi/10.1021/acs.macromol.0c00138
dcterms.rightsHolder.url
https://publish.acs.org/publish/author_guidelines?coden=mamobx#prior_publication_policy
refubium.affiliation
Physik
refubium.affiliation.other
Institut für Theoretische Physik
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refubium.resourceType.isindependentpub
no
dcterms.accessRights.openaire
open access
dcterms.isPartOf.eissn
0024-9297