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.

Raman spectra of 35 lipids are presented and analyzed in this work. Selected compounds, i.e. saturated/unsaturated fatty acids, triacylglycerols, cholesterol, cholesteryl esters and phospholipids, were chosen to review key lipids involved in cardiovascular disease development. Differences in Raman signatures both between diverse groups of lipids as well as various members of the same family are investigated in detail in order to elucidate marker features enabling detection and discrimination of lipids in complex samples, particularly of biological origin. This work complements our previous review on important biomolecules, i.e. proteins, and presents a comprehensive database of Raman spectra of naturally occurring lipids. Scheme 1. Chemical structure of chosen fatty acids: saturated (a) and unsaturated (b). Raman spectroscopy of lipids

No abstract

No abstract

This paper demonstrates the special advantages of FT-