FT-Raman spectra and charge densities of new anticonvulsant compounds

2001 ◽  
Vol 596 (1-3) ◽  
pp. 215-219
Author(s):  
A Wesełucha-Birczyńska ◽  
M Ciechanowicz-Rutkowska
Author(s):  
N. Sundaraganesan ◽  
S. Kalaichelvan ◽  
C. Meganathan ◽  
B. Dominic Joshua ◽  
J. Cornard

2000 ◽  
Vol 660 ◽  
Author(s):  
J. Casado ◽  
H. E. Katz ◽  
V. Hernández ◽  
J.T. López Navarrete

ABSTRACTIn this paper, the vibrational FT-Raman spectra obtained at different anodic potentials chosen in the oxidation and reduction branches of the voltamperometric waves of two α,α'-sexithiophenes end capped with n-hexyl and n-thiohexyl groups are investigated. In order to analyze the evolution of the atomic charges and bonth lengths on going from the neutral to the doped species some theoretical calculations have been carried out.


2019 ◽  
Vol 30 (4) ◽  
pp. 1025-1035
Author(s):  
B. Sathya ◽  
M. Prasath ◽  
M. Selvapandiyan ◽  
K. Prabha

2020 ◽  
Vol 1199 ◽  
pp. 126964 ◽  
Author(s):  
Maximiliano A. Iramain ◽  
María V. Castillo ◽  
Lilian Davies ◽  
María E. Manzur ◽  
Silvia Antonia Brandán

1992 ◽  
Vol 46 (10) ◽  
pp. 1503-1507 ◽  
Author(s):  
Y. Ozaki ◽  
R. Cho ◽  
K. Ikegaya ◽  
S. Muraishi ◽  
K. Kawauchi

The 1064-nm excited Fourier transform (FT) Raman spectra have been measured in situ for various foods in order to investigate the potential of near-infrared (NIR) FT-Raman spectroscopy in food analysis. It is demonstrated here that NIR FT-Raman spectroscopy is a very powerful technique for (1) detecting selectively the trace components in foodstuffs, (2) estimating the degree of unsaturation of fatty acids included in foods, (3) investigating the structure of food components, and (4) monitoring changes in the quality of foods. Carotenoids included in foods give two intense bands near 1530 and 1160 cm−1 via the pre-resonance Raman effect in the NIR FT-Raman spectra, and therefore, the NIR FT-Raman technique can be employed to detect them nondestructively. Foods consisting largely of lipids such as oils, tallow, and butter show bands near 1658 and 1443 cm−1 due to C=C stretching modes of cis unsaturated fatty acid parts and CH2 scissoring modes of saturated fatty acid parts, respectively. It has been found that there is a linear correlation for various kinds of lipid-containing foods between the iodine value (number) and the intensity ratio of two bands at 1658 and 1443 cm−1 ( I1658/ I1443), indicating that the ratio can be used as a practical indicator for estimating the unsaturation level of a wide range of lipid-containing foods. A comparison of the Raman spectra of raw and boiled egg white shows that the amide I band shifts from 1666 to 1677 cm−1 and the intensity of the amide III band at 1275 cm−1 decreases upon boiling. These observations indicate that most α-helix structure changes into unordered structure in the proteins constituting egg white upon boiling. The NIR FT-Raman spectrum of old-leaf (about one year old) Japanese tea has been compared with that of its new leaf. The intensity ratio of two bands at 1529 and 1446 cm−1 ( I1529/ I1446), assignable to carotenoid and proteins, respectively, is considerably smaller in the former than in the latter, indicating that the ratio is useful for monitoring the changes in the quality of Japanese tea.


Author(s):  
Tomislav Biljan ◽  
Sanda Rončević ◽  
Zlatko Meić ◽  
Kristina Jurčić ◽  
Ernest Meštrović
Keyword(s):  

Author(s):  
M. Alcolea Palafox ◽  
V. Bena Jothy ◽  
Surabhi Singhal ◽  
I. Hubert Joe ◽  
Satendra Kumar ◽  
...  

2020 ◽  
Vol 10 (17) ◽  
pp. 5918
Author(s):  
Azin Sadat ◽  
Iris J. Joye

FTIR and Raman spectroscopy are often used to investigate the secondary structure of proteins. Focus is then often laid on the different features that can be distinguished in the Amide I band (1600–1700 cm−1) and, to a lesser extent, the Amide II band (1510–1580 cm−1), signature regions for C=O stretching/N-H bending, and N-H bending/C-N stretching vibrations, respectively. Proper investigation of all hidden and overlapping features/peaks is a necessary step to achieve reliable analysis of FTIR and FT-Raman spectra of proteins. This paper discusses a method to identify, separate, and quantify the hidden peaks in the amide I band region of infrared and Raman spectra of four globular proteins in aqueous solution as well as hydrated zein and gluten proteins. The globular proteins studied, which differ widely in terms of their secondary structures, include immunoglobulin G, concanavalin A, lysozyme, and trypsin. Peak finding was done by analysis of the second derivative of the original spectra. Peak separation and quantification was achieved by curve fitting using the Voigt function. Structural data derived from the FT-Raman and FTIR analyses were compared to literature reports on protein structure. This manuscript proposes an accurate method to analyze protein secondary structure based on the amide I band in vibrational spectra.


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