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Portrait of Tönu Pullerits; Photo: Kennet Ruona

Tönu Pullerits

Professor

Portrait of Tönu Pullerits; Photo: Kennet Ruona

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

Author

  • Axel Schubert
  • Anna Stenstam
  • Wichard Beenken
  • Jennifer Herek
  • R Cogdell
  • Tönu Pullerits
  • Villy Sundström

Summary, in English

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.

Department/s

  • Chemical Physics
  • Physical Chemistry

Publishing year

2004

Language

English

Pages

2363-2373

Publication/Series

Biophysical Journal

Volume

86

Issue

4

Document type

Journal article

Publisher

Cell Press

Topic

  • Biophysics

Status

Published

ISBN/ISSN/Other

  • ISSN: 1542-0086