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Raman spectroscopy of proteins: from peptides to large assemblies

Tuma, Roman·2005·Journal of Raman Spectroscopy

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.

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Metadata

Authors
Tuma, R.
Venue
Journal of Raman Spectroscopy
Publisher
Wiley
Published
2005-04
Volume
36
Issue
4
Pages
307-319
ISSN
  • 0377-0486 (ISSN-L)
  • 1097-4555
OpenAlex
W2007879544
Cited by
460
References
0
FWCI
7.32
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Raman spectroscopy of proteins: from peptides to large assemblies. https://app.cochat.ai/papers/10.1002/jrs.1323
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Tuma, R. (2005). Raman spectroscopy of proteins: from peptides to large assemblies. Journal of Raman Spectroscopy. https://doi.org/10.1002/jrs.1323

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