Investigation of detergent effects on the solution structure of spinach Light Harvesting Complex II

Mateus B. Cardoso; Dmitriy Smolensky; William T. Heller; Hugh O'Neill

doi:10.1088/1742-6596/251/1/012041

Investigation of detergent effects on the solution structure of spinach Light Harvesting Complex II

Mateus B. Cardoso, Dmitriy Smolensky, William T. Heller, Hugh O'Neill

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Abstract

The properties of spinach light harvesting complex II (LHC II), stabilized in the detergents Triton X-100 (TX100) and n-Octyl-β-D-Glucoside (BOG), were investigated by small-angle neutron scattering (SANS). The LHC II-BOG scattering curve overlaid well with the theoretical scattering curve generated from the crystal structure of LHC II indicating that the protein preparation was in its native functional state. On the other hand, the simulated LHC II curve deviated significantly from the LHC II-TX100 experimental data. Analysis by circular dichroism spectroscopy supported the SANS analysis and showed that LHC II-TX100 is inactivated. This investigation has implications for extracting and stabilizing photosynthetic membrane proteins for the development of biohybrid photoconversion devices.

Original language	English
Article number	012041
Journal	Journal of Physics: Conference Series
Volume	251
Issue number	1
DOIs	https://doi.org/10.1088/1742-6596/251/1/012041
State	Published - 2010

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title = "Investigation of detergent effects on the solution structure of spinach Light Harvesting Complex II",

abstract = "The properties of spinach light harvesting complex II (LHC II), stabilized in the detergents Triton X-100 (TX100) and n-Octyl-β-D-Glucoside (BOG), were investigated by small-angle neutron scattering (SANS). The LHC II-BOG scattering curve overlaid well with the theoretical scattering curve generated from the crystal structure of LHC II indicating that the protein preparation was in its native functional state. On the other hand, the simulated LHC II curve deviated significantly from the LHC II-TX100 experimental data. Analysis by circular dichroism spectroscopy supported the SANS analysis and showed that LHC II-TX100 is inactivated. This investigation has implications for extracting and stabilizing photosynthetic membrane proteins for the development of biohybrid photoconversion devices.",

author = "Cardoso, {Mateus B.} and Dmitriy Smolensky and Heller, {William T.} and Hugh O'Neill",

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T1 - Investigation of detergent effects on the solution structure of spinach Light Harvesting Complex II

AU - Cardoso, Mateus B.

AU - Smolensky, Dmitriy

AU - Heller, William T.

AU - O'Neill, Hugh

PY - 2010

Y1 - 2010

N2 - The properties of spinach light harvesting complex II (LHC II), stabilized in the detergents Triton X-100 (TX100) and n-Octyl-β-D-Glucoside (BOG), were investigated by small-angle neutron scattering (SANS). The LHC II-BOG scattering curve overlaid well with the theoretical scattering curve generated from the crystal structure of LHC II indicating that the protein preparation was in its native functional state. On the other hand, the simulated LHC II curve deviated significantly from the LHC II-TX100 experimental data. Analysis by circular dichroism spectroscopy supported the SANS analysis and showed that LHC II-TX100 is inactivated. This investigation has implications for extracting and stabilizing photosynthetic membrane proteins for the development of biohybrid photoconversion devices.

AB - The properties of spinach light harvesting complex II (LHC II), stabilized in the detergents Triton X-100 (TX100) and n-Octyl-β-D-Glucoside (BOG), were investigated by small-angle neutron scattering (SANS). The LHC II-BOG scattering curve overlaid well with the theoretical scattering curve generated from the crystal structure of LHC II indicating that the protein preparation was in its native functional state. On the other hand, the simulated LHC II curve deviated significantly from the LHC II-TX100 experimental data. Analysis by circular dichroism spectroscopy supported the SANS analysis and showed that LHC II-TX100 is inactivated. This investigation has implications for extracting and stabilizing photosynthetic membrane proteins for the development of biohybrid photoconversion devices.

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SN - 1742-6588

VL - 251

JO - Journal of Physics: Conference Series

JF - Journal of Physics: Conference Series

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ER -

Investigation of detergent effects on the solution structure of spinach Light Harvesting Complex II

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