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Issue 11, 2009
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Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins

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Abstract

The introduction of time-resolved Fourier transform infrared (FT-IR) spectroscopy to biochemistry opened the possibility of monitoring the catalytic mechanism of proteins along their reaction pathways. The infrared approach is very fruitful, particularly in the application to membrane proteins where NMR and X-ray crystallography are challenged by the size and protein hydrophobicity, as well as by their limited time-resolution. Here, we summarize the principles and experimental realizations of time-resolved FT-IR spectroscopy developed in our group and compare with aspects emerging from other laboratories. Examples of applications to retinal proteins and energy transduction complexes are reviewed, which emphasize the impact of time-resolved FT-IR spectroscopy on the understanding of protein reactions on the level of single bonds.

Graphical abstract: Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins

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Publication details

The article was received on 06 Jul 2009, accepted on 14 Sep 2009 and first published on 06 Oct 2009


Article type: Perspective
DOI: 10.1039/B9PP00050J
Citation: Photochem. Photobiol. Sci., 2009,8, 1517-1528
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    Time-resolved methods in biophysics. 10. Time-resolved FT-IR difference spectroscopy and the application to membrane proteins

    I. Radu, M. Schleeger, C. Bolwien and J. Heberle, Photochem. Photobiol. Sci., 2009, 8, 1517
    DOI: 10.1039/B9PP00050J

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