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Protein Configuration Landscape Fluctuations Revealed by Exciton Transition Polarizations in Single Light Harvesting Complexes.

Tubasum, Sumera LU ; Torbjörnsson, Magne LU ; Yadav, Dheerendra LU ; Camacho Dejay, Rafael LU ; Söderlind, Gustaf LU ; Scheblykin, Ivan LU and Pullerits, Tönu LU (2016) In The Journal of Physical Chemistry Part B 120(4). p.724-732
Abstract
Protein is a flexible material with broad distribution of conformations forming an energy landscape of quasi-stationary states. Disentangling the system dynamics along this landscape is the key for understanding the functioning of the protein. Here we studied a photosynthetic antenna pigment-protein complex LH2 with single molecule two-dimensional polarization imaging. Modeling based on the Redfield relaxation theory well describes the observed polarization properties of LH2 fluorescence and fluorescence excitation, strongly suggesting that at 77 K the conformational subspace of the LH2 is limited to about three configurations with relatively frequent switching among each other. At room temperature the next level of fluctuations determines... (More)
Protein is a flexible material with broad distribution of conformations forming an energy landscape of quasi-stationary states. Disentangling the system dynamics along this landscape is the key for understanding the functioning of the protein. Here we studied a photosynthetic antenna pigment-protein complex LH2 with single molecule two-dimensional polarization imaging. Modeling based on the Redfield relaxation theory well describes the observed polarization properties of LH2 fluorescence and fluorescence excitation, strongly suggesting that at 77 K the conformational subspace of the LH2 is limited to about three configurations with relatively frequent switching among each other. At room temperature the next level of fluctuations determines the conformational dynamics. The results support the multitier model of the energy landscape of proteins and demonstrate the potential of the method for the studies of structural dynamics in proteins. (Less)
Please use this url to cite or link to this publication:
author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
The Journal of Physical Chemistry Part B
volume
120
issue
4
pages
724 - 732
publisher
The American Chemical Society
external identifiers
  • pmid:26741912
  • scopus:84957866190
  • wos:000369773100013
ISSN
1520-5207
DOI
10.1021/acs.jpcb.5b12466
language
English
LU publication?
yes
id
df543336-b1bd-4d9a-8889-4b4ae511c7f7 (old id 8592824)
date added to LUP
2016-02-10 13:47:48
date last changed
2017-02-13 13:10:01
@article{df543336-b1bd-4d9a-8889-4b4ae511c7f7,
  abstract     = {Protein is a flexible material with broad distribution of conformations forming an energy landscape of quasi-stationary states. Disentangling the system dynamics along this landscape is the key for understanding the functioning of the protein. Here we studied a photosynthetic antenna pigment-protein complex LH2 with single molecule two-dimensional polarization imaging. Modeling based on the Redfield relaxation theory well describes the observed polarization properties of LH2 fluorescence and fluorescence excitation, strongly suggesting that at 77 K the conformational subspace of the LH2 is limited to about three configurations with relatively frequent switching among each other. At room temperature the next level of fluctuations determines the conformational dynamics. The results support the multitier model of the energy landscape of proteins and demonstrate the potential of the method for the studies of structural dynamics in proteins.},
  author       = {Tubasum, Sumera and Torbjörnsson, Magne and Yadav, Dheerendra and Camacho Dejay, Rafael and Söderlind, Gustaf and Scheblykin, Ivan and Pullerits, Tönu},
  issn         = {1520-5207},
  language     = {eng},
  number       = {4},
  pages        = {724--732},
  publisher    = {The American Chemical Society},
  series       = {The Journal of Physical Chemistry Part B},
  title        = {Protein Configuration Landscape Fluctuations Revealed by Exciton Transition Polarizations in Single Light Harvesting Complexes.},
  url          = {http://dx.doi.org/10.1021/acs.jpcb.5b12466},
  volume       = {120},
  year         = {2016},
}