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In vitro self-assembly of the light harvesting pigment-protein LH2 revealed by ultrafast spectroscopy and electron microscopy

Schubert, Axel LU ; Stenstam, Anna LU ; Beenken, Wichard LU ; Herek, Jennifer LU ; Cogdell, R; Pullerits, Tönu LU and Sundström, Villy LU (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)
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author
organization
publishing date
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
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
2007-07-03 16:47:21
date last changed
2017-08-27 04:09:33
@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},
  volume       = {86},
  year         = {2004},
}