New methods for monitoring changes in proteins

Abstract

Two of the most important properties in the food context are the three‐dimensional structure and dynamical properties. These account for the structural and functional behavior of the proteins, and the manipulation of these during processing is an important part of food manufacture. One of the main tools for examining proteins is nuclear magnetic resonance (NMR). Historically this is long‐established but the advent of three‐ and four‐dimensional spectroscopy, together with the availability of very high magnetic fields, has opened up a new range of possibilities allowing the determination of solution‐state structure together with detailed dynamical information. At the same time, relaxation time and solid‐state measurements can give useful information about proteins in solid and quasi‐solid systems. The vibrational spectra of proteins are potentially a rich source of structural information. In the past both infrared and Raman methods have been difficult to apply. Infrared has suffered from