Raman spectroscopy of proteins: from peptides to large assemblies
Article first published online: 15 APR 2005
Copyright © 2005 John Wiley & Sons, Ltd.
Journal of Raman Spectroscopy
Special Issue: Structure and dynamics of biomolecules
Volume 36, Issue 4, pages 307–319, April 2005
How to Cite
Tuma, R. (2005), Raman spectroscopy of proteins: from peptides to large assemblies. J. Raman Spectrosc., 36: 307–319. doi: 10.1002/jrs.1323
- Issue published online: 15 APR 2005
- Article first published online: 15 APR 2005
- Manuscript Accepted: 2 FEB 2005
- Manuscript Received: 18 JAN 2005
- Academy of Finland.. Grant Number: 206926.
- Finnish Centre of Excellence Program 2000–2005.
- protein folding;
- amide modes;
- enzyme–substrate interaction;
- Raman difference spectroscopy
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.