Coupling of a Microfluidic Mixer to a Fourier-transform Infrared Spectrometer for Protein-Conformation Studies
FH – HES
DOI:
https://doi.org/10.2533/chimia.2011.815Keywords:
Ftir, Microfluidic, Protein conformation, Protein foldingAbstract
The biological properties of a protein critically depend on its conformation, which can vary as a result of changes in conditions such as pH or following the addition of various substances. Being able to reliably assess the quality of protein structures under various conditions is therefore of crucial importance. Infrared (IR) spectroscopy of the Amide I band of proteins is a powerful method for the determination of protein conformations and further allows the analysis of continuously flowing solutions of the target molecule. Here, a commercial Fourier-transform infrared spectrometer was coupled to a microfluidic mixer to allow the on-line monitoring of protein conformation under varying conditions. The validity of the concept was demonstrated by continuously recording the variations of the IR spectrum of poly-L-lysine resulting from repetitive, pH-induced conformational changes.Downloads
Published
2011-10-26
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Copyright (c) 2011 Swiss Chemical Society
This work is licensed under a Creative Commons Attribution-NonCommercial 4.0 International License.
How to Cite
[1]
Chimia 2011, 65, 815, DOI: 10.2533/chimia.2011.815.