Characterization of protein structure and stability using Fourier transform infrared spectroscopy.

Abstract

Fourier transform infrared (FTIR) spectroscopy has recently emerged as a popular technique in the reld of analytical biotechnology. It is one of the few approaches that can be used to probe protein conformational changes in a wide range of environments including aqueous solution and the solid state, as well as in the presence of detergents, micelles, membranes and organic solvents. It is particularly useful for monitoring secondary structural changes in proteins through the analysis of the Amide I band. Information on protein dynamics can be derived through the study of hydrogen-deuterium exchange using the Amide II band. Changes in protein structure and stability as a function of temperature can also be readily investigated. The advantages of FTIR spectroscopy for structure and stability studies of peptides and proteins are presented.