title: Coupling of a microfluidic mixer to a Fourier-transform infrared spectrometer for protein-conformation studies.
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.
authors: HES-SO Valais, Institute of Life Technologies, Route du Rawyl 47, CH-1950 Sion 2, Switzerland.
authors: Denis
authors: D
authors: Prim
authors: Simon
authors: S
authors: Crelier
authors: Jean-Manuel
authors: JM
authors: Segura
mesh_terms: D004867:Equipment Design; D006454:Hemoglobins / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D046210:Microfluidic Analytical Techniques; D044085:Microfluidics; D011107:Polylysine / Q000737:chemistry; D011487:Protein Conformation; D017510:Protein Folding; D011506:Proteins / Q000737:chemistry*; D013055:Spectrophotometry, Infrared / Q000379:methods*; D017550:Spectroscopy, Fourier Transform Infrared / Q000379:methods*
chemical_list: D006454:Hemoglobins; D011506:Proteins; D011107:Polylysine