In vitro self-assembly of the light harvesting pigment-protein LH2 revealed by ultrafast spectroscopy and electron microscopy
(2004) In Biophysical Journal 86(4). p.2363-2373- Abstract
- Controlled ensemble formation of protein-surfactant systems provides a fundamental concept for the realization of nanoscale devices with self-organizing capability. In this context, spectroscopic monitoring of pigment-containing proteins yields detailed structural information. Here we have studied the association behavior of the bacterial light-harvesting protein LH2 from Rhodobacter spheroides in an n,n-dimethyldodecylamine-n-oxide/water environment. Time-resolved studies of the excitation annihilation yielded information about aggregate sizes and packing of the protein complexes therein. The results are compared to transmission electron microscopy images of instantaneously frozen samples. Our data indicate the manifestation of different... (More)
- Controlled ensemble formation of protein-surfactant systems provides a fundamental concept for the realization of nanoscale devices with self-organizing capability. In this context, spectroscopic monitoring of pigment-containing proteins yields detailed structural information. Here we have studied the association behavior of the bacterial light-harvesting protein LH2 from Rhodobacter spheroides in an n,n-dimethyldodecylamine-n-oxide/water environment. Time-resolved studies of the excitation annihilation yielded information about aggregate sizes and packing of the protein complexes therein. The results are compared to transmission electron microscopy images of instantaneously frozen samples. Our data indicate the manifestation of different phases, which are discussed with respect to the thermodynamic equilibrium in ternary protein-surfactant-water systems. Accordingly, by varying the concentration the formation of different types of aggregates can be controlled. Conditions for the appearance of isolated LH2 complexes are defined. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/139064
- author
- Schubert, Axel LU ; Stenstam, Anna LU ; Beenken, Wichard LU ; Herek, Jennifer LU ; Cogdell, R ; Pullerits, Tönu LU and Sundström, Villy LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Biophysical Journal
- volume
- 86
- issue
- 4
- pages
- 2363 - 2373
- publisher
- Cell Press
- external identifiers
-
- wos:000220567600040
- pmid:15041674
- scopus:1942423239
- ISSN
- 1542-0086
- 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: Physical Chemistry 1 (S) (011001006), Chemical Physics (S) (011001060)
- id
- 7d0eea48-69be-43c2-b1d5-73433d9e8c34 (old id 139064)
- alternative location
- http://www.pubmedcentral.gov/articlerender.fcgi?artid=1304085&rendertype=abstract
- http://www.biophysj.org/cgi/content/abstract/86/4/2363
- date added to LUP
- 2016-04-01 12:12:27
- date last changed
- 2022-01-27 00:27:22
@article{7d0eea48-69be-43c2-b1d5-73433d9e8c34,
abstract = {{Controlled ensemble formation of protein-surfactant systems provides a fundamental concept for the realization of nanoscale devices with self-organizing capability. In this context, spectroscopic monitoring of pigment-containing proteins yields detailed structural information. Here we have studied the association behavior of the bacterial light-harvesting protein LH2 from Rhodobacter spheroides in an n,n-dimethyldodecylamine-n-oxide/water environment. Time-resolved studies of the excitation annihilation yielded information about aggregate sizes and packing of the protein complexes therein. The results are compared to transmission electron microscopy images of instantaneously frozen samples. Our data indicate the manifestation of different phases, which are discussed with respect to the thermodynamic equilibrium in ternary protein-surfactant-water systems. Accordingly, by varying the concentration the formation of different types of aggregates can be controlled. Conditions for the appearance of isolated LH2 complexes are defined.}},
author = {{Schubert, Axel and Stenstam, Anna and Beenken, Wichard and Herek, Jennifer and Cogdell, R and Pullerits, Tönu and Sundström, Villy}},
issn = {{1542-0086}},
language = {{eng}},
number = {{4}},
pages = {{2363--2373}},
publisher = {{Cell Press}},
series = {{Biophysical Journal}},
title = {{In vitro self-assembly of the light harvesting pigment-protein LH2 revealed by ultrafast spectroscopy and electron microscopy}},
url = {{https://lup.lub.lu.se/search/files/2826825/624735.pdf}},
volume = {{86}},
year = {{2004}},
}