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Electronic circular dichroism of fluorescent proteins: A computational study

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https://hdl.handle.net/10037/24753
DOI
https://doi.org/10.1021/jp511199g
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Accepted manuscript version (PDF)
Date
2015-02-03
Type
Journal article
Tidsskriftartikkel
Peer reviewed

Author
Pikulska, Anna; Steindal, Arnfinn Hykkerud; Beerepoot, Maarten; Pecul, Magdalena
Abstract
The 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.
Description
This 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 https://doi.org/10.1021/jp511199g.
Publisher
American Chemical Society
Citation
Pikulska A, Steindal AHS, Beerepoot MTP, Pecul M. Electronic circular dichroism of fluorescent proteins: A computational study. Journal of Physical Chemistry B. 2015;119(8):3377-3386
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