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dc.contributor.authorPikulska, Anna
dc.contributor.authorSteindal, Arnfinn Hykkerud
dc.contributor.authorBeerepoot, Maarten
dc.contributor.authorPecul, Magdalena
dc.date.accessioned2022-04-11T13:38:13Z
dc.date.available2022-04-11T13:38:13Z
dc.date.issued2015-02-03
dc.description.abstractThe electronic circular dichroism (ECD) properties of the green fluorescent protein and other fluorescent proteins have been calculated with density functional theory. The influence of different embedding models on the ECD signal of the chromophore has been investigated by modeling the protein environment by the polarizable continuum model (QM/PCM), by the polarizable embedding model (PE-QM/MM), by treating the minimal environment quantum mechanically at the same footing as the chromophore (QM/QM), and by adding the remaining part of the protein by means of PCM (QM/QM/PCM). The rotatory strength is found to be more sensitive than the oscillatory strength to changes in the geometry of the chromophore and its surroundings and to the type of embedding model used. In general, explicit embedding of the surrounding protein (PE-QM/MM or QM/QM) induces an increase in the rotatory strength of the chromophore. Explicit inclusion of the whole protein through polarizable embedding is found to be an affordable embedding model that gives the correct sign of the rotatory strength for all fluorescent proteins. PCM is useful as a first approximation to protein environment effects, but as a rule seems to underestimate the rotatory strength.en_US
dc.descriptionThis document is the Accepted Manuscript version of a Published Work that appeared in final form in Journal of Physical Chemistry B, Copyright © 2015 American Chemical Society after peer review and technical editing by the publisher. To access the final edited and published work see <a href=https://doi.org/10.1021/jp511199g>https://doi.org/10.1021/jp511199g</a>.en_US
dc.identifier.citationPikulska A, Steindal AHS, Beerepoot MTP, Pecul M. Electronic circular dichroism of fluorescent proteins: A computational study. Journal of Physical Chemistry B. 2015;119(8):3377-3386en_US
dc.identifier.cristinIDFRIDAID 1252418
dc.identifier.doi10.1021/jp511199g
dc.identifier.issn1520-6106
dc.identifier.issn1520-5207
dc.identifier.urihttps://hdl.handle.net/10037/24753
dc.language.isoengen_US
dc.publisherAmerican Chemical Societyen_US
dc.relation.journalJournal of Physical Chemistry B
dc.relation.projectIDNorges forskningsråd: 179568en_US
dc.relation.projectIDNotur/NorStore: NN4654Ken_US
dc.relation.projectIDEU: 279619en_US
dc.relation.projectIDinfo:eu-repo/grantAgreement/EC/FP7/279619/Norway/Theoretical multiphoton spectroscopy for understanding surfaces and interfaces/SURFSPSEC/en_US
dc.rights.accessRightsopenAccessen_US
dc.rights.holderCopyright 2015 The Author(s)en_US
dc.titleElectronic circular dichroism of fluorescent proteins: A computational studyen_US
dc.type.versionacceptedVersionen_US
dc.typeJournal articleen_US
dc.typeTidsskriftartikkelen_US
dc.typePeer revieweden_US


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