Format

Send to

Choose Destination
See comment in PubMed Commons below
Chimia (Aarau). 2011;65(10):815-6. doi: 10.2533/chimia.2011.815.

Coupling of a microfluidic mixer to a Fourier-transform infrared spectrometer for protein-conformation studies.

Author information

  • 1HES-SO Valais, Institute of Life Technologies, Route du Rawyl 47, CH-1950 Sion 2, Switzerland.

Abstract

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.

[PubMed - indexed for MEDLINE]
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Ingenta plc
    Loading ...
    Write to the Help Desk