2013/07/13 by A. Rygula, Anna Ryguła, K. Majzner +9 · 10 citations
Biochemistry, Genetics and Molecular Biology · Chemistry · #Molecular spectroscopy and chirality #Protein Interaction Studies and Fluorescence Analysis #Spectroscopy Techniques in Biomedical and Chemical Research
paper · doi:10.1002/jrs.4335
openalex publication_date 2013/07/13 · openalex created_date 2016/06/24 · openalex updated_date 2026/07/28
In this work, 26 proteins of different structure, function and properties are investigated by Raman spectroscopy with 488, 532 and 1064 nm laser lines. The excitation lines were chosen in NIR and Vis range as the most common and to show the difference due to normal and resonance effect, sometimes accompanied by the fluorescence. The selected proteins were divided, according to the Structural Classification of Proteins, into four classes according to their secondary structure, i.e. α‐helical (α), β‐sheet (β), mixed structures (α/β, α + β, s) and others. For all compounds, FT‐Raman and two Vis spectra are presented along with the detailed band assignment. To the best of our knowledge, this is the first review showing the potential of Raman spectroscopy for the measurement and analysis of such a large collection of individual proteins. This work can serve as a comprehensive vibrational spectra library, based on our and previous Raman measurements. Copyright © 2013 John Wiley & Sons, Ltd.