Protein Influence on Electronic Spectra Modeled by Multipoles and Polarizabilities
Söderhjelm, Pär LU ; Husberg, Charlotte ; Strambi, Angela ; Olivucci, Massimo and Ryde, Ulf LU
(2009)
In Journal of Chemical Theory and Computation
5(3).
p.649-658
- Abstract
- We have developed automatic methods to calculate multipoles and anisotropic polarizabilities for all atoms and bond centers in a protein and to include such a model in the calculation of electronic properties at any level of quantum mechanical theory. This approach is applied for the calculation of the electronic spectra of retinal in rhodopsin at the CASPT2//CASSCF level (second-order multiconfigurational perturbation theory) for the wild-type protein, as well as two mutants and isorhodopsin in QM/MM structures based on two crystal structures. We also perform a detailed investigation of the importance and distance dependence of the multipoles and the polarizabilities for both the absolute and the relative absorption energies. It is shown... (More)
- We have developed automatic methods to calculate multipoles and anisotropic polarizabilities for all atoms and bond centers in a protein and to include such a model in the calculation of electronic properties at any level of quantum mechanical theory. This approach is applied for the calculation of the electronic spectra of retinal in rhodopsin at the CASPT2//CASSCF level (second-order multiconfigurational perturbation theory) for the wild-type protein, as well as two mutants and isorhodopsin in QM/MM structures based on two crystal structures. We also perform a detailed investigation of the importance and distance dependence of the multipoles and the polarizabilities for both the absolute and the relative absorption energies. It is shown that the model of the surrounding protein strongly influences the spectrum and that different models give widely different results. For example, the Amber 1994 and 2003 force fields give excitation energies that differ by up to 16 kJ/mol. For accurate excitation energies, multipoles up to quadrupoles and anisotropic polarizabilities are needed. However, interactions with residues more than 10 A from the chromophore can be treated with a standard polarizable force field without any dipoles or quadrupoles. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/1404851
- author
- Söderhjelm, Pär
LU
; Husberg, Charlotte
; Strambi, Angela
; Olivucci, Massimo
and Ryde, Ulf
LU
- organization
- publishing date
- 2009
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Chemical Theory and Computation
- volume
- 5
- issue
- 3
- pages
- 649 - 658
- publisher
- The American Chemical Society (ACS)
- external identifiers
-
- wos:000264085600021
- scopus:65349179259
- pmid:26610229
- ISSN
- 1549-9618
- DOI
- 10.1021/ct800459t
- language
- English
- LU publication?
- yes
- additional info
- The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Theoretical Chemistry (S) (011001039)
- id
- 919a5777-96ad-4b91-902b-ce01917d0389 (old id 1404851)
- date added to LUP
- 2016-04-01 11:46:40
- date last changed
- 2023-02-07 02:35:13
@article{919a5777-96ad-4b91-902b-ce01917d0389,
abstract = {{We have developed automatic methods to calculate multipoles and anisotropic polarizabilities for all atoms and bond centers in a protein and to include such a model in the calculation of electronic properties at any level of quantum mechanical theory. This approach is applied for the calculation of the electronic spectra of retinal in rhodopsin at the CASPT2//CASSCF level (second-order multiconfigurational perturbation theory) for the wild-type protein, as well as two mutants and isorhodopsin in QM/MM structures based on two crystal structures. We also perform a detailed investigation of the importance and distance dependence of the multipoles and the polarizabilities for both the absolute and the relative absorption energies. It is shown that the model of the surrounding protein strongly influences the spectrum and that different models give widely different results. For example, the Amber 1994 and 2003 force fields give excitation energies that differ by up to 16 kJ/mol. For accurate excitation energies, multipoles up to quadrupoles and anisotropic polarizabilities are needed. However, interactions with residues more than 10 A from the chromophore can be treated with a standard polarizable force field without any dipoles or quadrupoles.}},
author = {{Söderhjelm, Pär and Husberg, Charlotte and Strambi, Angela and Olivucci, Massimo and Ryde, Ulf}},
issn = {{1549-9618}},
language = {{eng}},
number = {{3}},
pages = {{649--658}},
publisher = {{The American Chemical Society (ACS)}},
series = {{Journal of Chemical Theory and Computation}},
title = {{Protein Influence on Electronic Spectra Modeled by Multipoles and Polarizabilities}},
url = {{https://lup.lub.lu.se/search/files/136744686/121_rhodopsin.pdf}},
doi = {{10.1021/ct800459t}},
volume = {{5}},
year = {{2009}},
}