Protein Configuration Landscape Fluctuations Revealed by Exciton Transition Polarizations in Single Light Harvesting Complexes.
(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:
https://lup.lub.lu.se/record/8592824
- author
- Tubasum, Sumera LU ; Torbjörnsson, Magne LU ; Yadav, Dheerendra LU ; Camacho Dejay, Rafael LU ; Söderlind, Gustaf LU ; Scheblykin, Ivan LU and Pullerits, Tönu LU
- organization
- publishing date
- 2016
- 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 (ACS)
- external identifiers
-
- pmid:26741912
- scopus:84957866190
- wos:000369773100013
- pmid:26741912
- 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
- 2016-04-01 13:37:23
- date last changed
- 2022-04-02 12:29:10
@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 (ACS)}}, 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}}, doi = {{10.1021/acs.jpcb.5b12466}}, volume = {{120}}, year = {{2016}}, }