“…Table 5 shows the assignments. [ 1,58–60 ] The ν (CS) of Met is at 656 cm −1 . Moreover, the NH 3 + group shows clear HR bands: ν as (NH 3 + ) and δ (NH 3 + ) around 1,644 cm −1 and ρ (NH 3 + ) at 996 cm −1 .…”
This paper reports the hyper‐Raman (HR) spectra of the 20 amino acids in aqueous solution in the range of 400–1,800 cm−1 with an excitation wavelength of 532 nm. A remarkable common feature in the nonresonance HR spectra is the large intensity of the HR bands of the COO− group. Whereas the peak position is mostly identical between the HR and Raman spectra, the intensity pattern is not. We discuss the similarities and dissimilarities between the pattern of the two spectra of each amino acid and give possible assignments to each HR band by comparing them with those of the corresponding Raman band. This study offers a reference for the HR spectra of the amino acids as the basic building block of proteins. It helps interpret the HR spectra of proteins and peptides.
“…Table 5 shows the assignments. [ 1,58–60 ] The ν (CS) of Met is at 656 cm −1 . Moreover, the NH 3 + group shows clear HR bands: ν as (NH 3 + ) and δ (NH 3 + ) around 1,644 cm −1 and ρ (NH 3 + ) at 996 cm −1 .…”
This paper reports the hyper‐Raman (HR) spectra of the 20 amino acids in aqueous solution in the range of 400–1,800 cm−1 with an excitation wavelength of 532 nm. A remarkable common feature in the nonresonance HR spectra is the large intensity of the HR bands of the COO− group. Whereas the peak position is mostly identical between the HR and Raman spectra, the intensity pattern is not. We discuss the similarities and dissimilarities between the pattern of the two spectra of each amino acid and give possible assignments to each HR band by comparing them with those of the corresponding Raman band. This study offers a reference for the HR spectra of the amino acids as the basic building block of proteins. It helps interpret the HR spectra of proteins and peptides.
“…Among these properties we can cite polymorphism [1] and phase transitions [2][3][4][5][6][7][8][9][10]. It is known that certain proteic amino acid crystals present polymorphism when subject to high pressures: L-cysteine [3][4][5],L-serine [6][7][8], methionine-including the L- [9] and the D-forms [10], among others. On the other hand, a-glycine seems to be stable up to 23 GPa, as a Raman spectroscopic investigation has revealed [11].…”
We report a very simple, rapid and reproducible method for the fabrication of anisotropic silver nanostars (AgNS) that can be successfully used as highly efficient SERS substrates for different bioanalytes, even in the case of a near-infra-red (NIR) excitation laser. The nanostars have been synthesized using the chemical reduction of Ag+ ions by trisodium citrate. This is the first research reporting the synthesis of AgNS using only trisodium citrate as a reducing and stabilizing agent. The key elements of this original synthesis procedure are rapid hydrothermal synthesis of silver nanostars followed by a cooling down procedure by immersion in a water bath. The synthesis was performed in a sealed bottom flask homogenously heated and brought to a boil in a microwave oven. After 60 s, the colloidal solution was cooled down to room temperature by immersion in a water bath at 35 °C. The as-synthesized AgNS were washed by centrifugation and used for SERS analysis of test molecules (methylene blue) as well as biological analytes: pharmaceutical compounds with various Raman cross sections (doxorubicin, atenolol & metoprolol), cell lysates and amino acids (methionine & cysteine). UV-Vis absorption spectroscopy, (Scanning) Transmission Electron Microscopy ((S)TEM) and Atomic Force Microscopy (AFM) have been employed for investigating nanostars’ physical properties.
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