Raman spectroscopy of proteins: from peptides to large assemblies

TLDR

Raman spectroscopy is a versatile tool in protein science and biotechnology, used to characterize intrinsically unstructured proteins. Recent advances in spectral assignments, vibrational theory, and instrument sensitivity enable Raman difference spectroscopy to probe enzyme–substrate interactions and are applied in structural biology and industry. Classical Raman spectroscopy provides new insights into protein folding, assembly, and aggregation, while Raman crystallography reveals protein–ligand interactions with higher resolution than X‑ray diffraction, and commercial instruments have expanded its applications in biotechnology and the food industry. © 2005 John Wiley & Sons, Ltd.

Abstract

Abstract Raman spectroscopy has become a versatile tool in protein science and biotechnology. Recent advances in spectral assignments and vibrational theory, examples of use in structural biology and selected industrial applications are discussed. New insights into protein folding, assembly and aggregation were obtained by classical Raman spectroscopy. Raman spectroscopy has been used to characterize intrinsically unstructured proteins. The improved instrument sensitivity made it possible to use Raman difference spectroscopy to characterize enzyme–substrate interactions. Specifically, Raman crystallography has been instrumental in the delineation of protein–ligand interactions with a resolution surpassing that of x‐ray diffraction. Numerous applications of Raman spectroscopy to protein analysis in biotechnology and food industry have been facilitated by the new generation of commercial Raman instruments. Copyright © 2005 John Wiley & Sons, Ltd.