Journal of Physical Chemistry B, volume 117, issue 43, pages 13507-13514
Thermal isomerization of the chromoprotein asFP595 and its kindling mutant A143G: QM/MM molecular dynamics simulations
Publication type: Journal Article
Publication date: 2013-10-15
Journal:
Journal of Physical Chemistry B
Quartile SCImago
Q1
Quartile WOS
Q3
Impact factor: 3.3
ISSN: 15206106, 15205207
Materials Chemistry
Surfaces, Coatings and Films
Physical and Theoretical Chemistry
Abstract
Chromoprotein asFP595 and its A143G variant called kindling fluorescent protein (KFP) are among the chronologically first species for which trans-cis chromophore isomerization has been proposed as a driving force of photoswitching. In spite of long-lasting efforts to characterize the route between protein conformations referring to the trans and cis forms of the chromophore, the molecular mechanism of this transformation is still under debate. We report the results of computational studies of the trans-cis isomerization of the anionic and neutral chromophore inside the protein matrices in the ground electronic state for both variants, asFP595 and KFP. Corresponding free energy profiles (potentials of mean force) were evaluated by using molecular dynamics simulations with the quantum mechanical-molecular mechanical (QM/MM) forces. The computed free energy barrier for the cis-trans ground state (thermal) isomerization reaction is about 2 kcal/mol higher in KFP than that in asFP595. These results provide interpretation of experimental studies on thermal relaxation from the light-induced activation of fluorescence of these proteins and correctly show that the A143G mutation in asFP595 noticeably increases the lifetime of the fluorescence species.
Citations by journals
|
1
2
3
4
|
|
|
Journal of Physical Chemistry B
|
Journal of Physical Chemistry B
4 publications, 44.44%
|
|
Chemical Reviews
|
Chemical Reviews
1 publication, 11.11%
|
|
International Journal of Molecular Sciences
|
International Journal of Molecular Sciences
1 publication, 11.11%
|
|
Computational Biology and Chemistry
|
Computational Biology and Chemistry
1 publication, 11.11%
|
|
Journal of Physical Chemistry A
|
Journal of Physical Chemistry A
1 publication, 11.11%
|
|
1
2
3
4
|
Citations by publishers
|
1
2
3
4
5
6
|
|
|
American Chemical Society (ACS)
|
American Chemical Society (ACS)
6 publications, 66.67%
|
|
Multidisciplinary Digital Publishing Institute (MDPI)
|
Multidisciplinary Digital Publishing Institute (MDPI)
1 publication, 11.11%
|
|
Elsevier
|
Elsevier
1 publication, 11.11%
|
|
1
2
3
4
5
6
|
- We do not take into account publications that without a DOI.
- Statistics recalculated only for publications connected to researchers, organizations and labs registered on the platform.
- Statistics recalculated weekly.
{"yearsCitations":{"type":"bar","data":{"show":true,"labels":[2014,2015,2016,2017,2018,2019,2020,2021,2022,2023,2024],"ids":[0,0,0,0,0,0,0,0,0,0,0],"codes":[0,0,0,0,0,0,0,0,0,0,0],"imageUrls":["","","","","","","","","","",""],"datasets":[{"label":"Citations number","data":[1,1,2,0,0,2,0,1,0,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":["11.11","11.11","22.22",0,0,"22.22",0,"11.11",0,"11.11","11.11"],"barThickness":null}]},"options":{"indexAxis":"x","maintainAspectRatio":true,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":1,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Citations per year","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"journals":{"type":"bar","data":{"show":true,"labels":["Journal of Physical Chemistry B","Chemical Reviews","International Journal of Molecular Sciences","Computational Biology and Chemistry","Journal of Physical Chemistry A"],"ids":[14990,13718,14627,16827,15255],"codes":[0,0,0,0,0],"imageUrls":["\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/MjH1ITP7lMYGxeqUZfkt2BnVLgjkk413jwBV97XX_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp","\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp"],"datasets":[{"label":"","data":[4,1,1,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6","#3B82F6","#3B82F6"],"percentage":[44.44,11.11,11.11,11.11,11.11],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Journals","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}},"publishers":{"type":"bar","data":{"show":true,"labels":["American Chemical Society (ACS)","Multidisciplinary Digital Publishing Institute (MDPI)","Elsevier"],"ids":[40,202,17],"codes":[0,0,0],"imageUrls":["\/storage\/images\/resized\/iLiQsFqFaSEx6chlGQ5fbAwF6VYU3WWa08hkss0g_medium.webp","\/storage\/images\/resized\/MjH1ITP7lMYGxeqUZfkt2BnVLgjkk413jwBV97XX_medium.webp","\/storage\/images\/resized\/GDnYOu1UpMMfMMRV6Aqle4H0YLLsraeD9IP9qScG_medium.webp"],"datasets":[{"label":"","data":[6,1,1],"backgroundColor":["#3B82F6","#3B82F6","#3B82F6"],"percentage":[66.67,11.11,11.11],"barThickness":13}]},"options":{"indexAxis":"y","maintainAspectRatio":false,"scales":{"y":{"ticks":{"precision":0,"autoSkip":false,"font":{"family":"Montserrat"},"color":"#000000"}},"x":{"ticks":{"stepSize":null,"precision":0,"font":{"family":"Montserrat"},"color":"#000000"}}},"plugins":{"legend":{"position":"top","labels":{"font":{"family":"Montserrat"},"color":"#000000"}},"title":{"display":true,"text":"Publishers","font":{"size":24,"family":"Montserrat","weight":600},"color":"#000000"}}}}}
Metrics
Cite this
GOST |
RIS |
BibTex |
MLA
Cite this
GOST
Copy
Mironov V. et al. Thermal isomerization of the chromoprotein asFP595 and its kindling mutant A143G: QM/MM molecular dynamics simulations // Journal of Physical Chemistry B. 2013. Vol. 117. No. 43. pp. 13507-13514.
GOST all authors (up to 50)
Copy
Mironov V., Khrenova M. G., Grigorenko B., Savitsky A., Nemukhin A. Thermal isomerization of the chromoprotein asFP595 and its kindling mutant A143G: QM/MM molecular dynamics simulations // Journal of Physical Chemistry B. 2013. Vol. 117. No. 43. pp. 13507-13514.
Cite this
RIS
Copy
TY - JOUR
DO - 10.1021/jp407406k
UR - https://doi.org/10.1021%2Fjp407406k
TI - Thermal isomerization of the chromoprotein asFP595 and its kindling mutant A143G: QM/MM molecular dynamics simulations
T2 - Journal of Physical Chemistry B
AU - Mironov, Vladimir
AU - Khrenova, Maria G.
AU - Grigorenko, Bella
AU - Savitsky, Alexander
AU - Nemukhin, Alexander
PY - 2013
DA - 2013/10/15 00:00:00
PB - American Chemical Society (ACS)
SP - 13507-13514
IS - 43
VL - 117
SN - 1520-6106
SN - 1520-5207
ER -
Cite this
BibTex
Copy
@article{2013_Mironov,
author = {Vladimir Mironov and Maria G. Khrenova and Bella Grigorenko and Alexander Savitsky and Alexander Nemukhin},
title = {Thermal isomerization of the chromoprotein asFP595 and its kindling mutant A143G: QM/MM molecular dynamics simulations},
journal = {Journal of Physical Chemistry B},
year = {2013},
volume = {117},
publisher = {American Chemical Society (ACS)},
month = {oct},
url = {https://doi.org/10.1021%2Fjp407406k},
number = {43},
pages = {13507--13514},
doi = {10.1021/jp407406k}
}
Cite this
MLA
Copy
Mironov, Vladimir, et al. “Thermal isomerization of the chromoprotein asFP595 and its kindling mutant A143G: QM/MM molecular dynamics simulations.” Journal of Physical Chemistry B, vol. 117, no. 43, Oct. 2013, pp. 13507-13514. https://doi.org/10.1021%2Fjp407406k.