Raman Optical Activity on a Solid Sample: Identification of Atropisomers of Perfluoroalkyl Chains Having a Helical Conformation and No Chiral Center

2019 ◽  
Vol 123 (18) ◽  
pp. 3985-3991 ◽  
Author(s):  
Takafumi Shimoaka ◽  
Masashi Sonoyama ◽  
Hideki Amii ◽  
Toshiyuki Takagi ◽  
Toshiyuki Kanamori ◽  
...  
Keyword(s):  
Optical Activity ◽  
Solid Sample ◽  
Chiral Center ◽  
Helical Conformation ◽  
Raman Optical Activity ◽  
Sample Identification

scholarly journals Raman optical activity study of poly-L-proline chains of various lengths

2010 ◽  
Vol 24 (3-4) ◽  
pp. 213-217 ◽  
Author(s):  
V. Profant ◽  
M. Šafarík ◽  
P. Bour ◽  
V. Baumruk
Keyword(s):  
Optical Activity ◽  
Conformational Stability ◽  
High Sensitivity ◽  
Wide Frequency Range ◽  
Peptide Chain ◽  
Helical Conformation ◽  
Polyproline Ii ◽  
Raman Optical Activity ◽  
Spectral Peaks ◽  
Chain Lengths

Raman and Raman optical activity (ROA) spectra of several oligo- and poly-L-proline samples of various chain lengths were measured in a wide frequency range between 120 and 1800 cm−1and analysed with respect to the main peptide chain conformation. Specifically, formation of polyproline II (PPII) helical conformation was studied in dependence on the increasing chain lengthNof the (L-proline)Nsample. Due to high sensitivity of the ROA technique to the conformational stability and rigidity of peptide chain we were able to determine the characteristic spectral peaks associated with formation of stable PPII helical conformation in studied systems. The most relevant peaks are located at 405, 535 and 945 cm−1. Additionally, based on our data analysis, we were able to determine the minimal length of (L-proline)Nchain necessary for creation of the stable PPII conformation asN= 6.

Raman Optical Activity of the Central Part of Hinge Peptide

2005 ◽  
Vol 70 (4) ◽  
pp. 403-409 ◽  
Author(s):  
Josef Kapitán ◽  
Vladimír Baumruk ◽  
Vladimír Gut ◽  
Jan Hlaváček ◽  
Helena Dlouhá ◽  
...  
Keyword(s):  
Optical Activity ◽  
Disulfide Bonds ◽  
Vibrational Circular Dichroism ◽  
Helical Conformation ◽  
Disulfide Bridges ◽  
Polyproline Ii ◽  
Raman Optical Activity ◽  
Stretching Vibration ◽  
Human Igg1 ◽  
Cyclic Part

Central cyclic part of the hinge peptide (a parallel dimer of the pentapeptide Boc-Cys-Pro-Pro-Cys-Pro-NHCH3 with two disulfide bonds) derived from the sequence of human IgG1 is a rather rigid structure having predominantly polyproline II helical conformation as shown by vibrational circular dichroism spectra. It exhibits significant Raman optical activity (ROA) signal due to vibrations associated with the disulfide bridges. We report positive ROA for the S-S stretching vibration at 510 cm-1 and for the C-S stretching vibration at 655 cm-1. These signals can provide means to assess the conformation of disulfide bridges in proteins, otherwise difficult to investigate.

scholarly journals Molecular structures of viruses from Raman optical activity

2002 ◽  
Vol 83 (10) ◽  
pp. 2593-2600 ◽  
Author(s):  
Ewan W. Blanch ◽  
Lutz Hecht ◽  
Christopher D. Syme ◽  
Vito Volpetti ◽  
George P. Lomonossoff ◽  
...  
Keyword(s):  
Tobacco Mosaic Virus ◽  
Mosaic Virus ◽  
Optical Activity ◽  
Molecular Structures ◽  
Helical Conformation ◽  
Amino Acid Side Chain ◽  
Cowpea Mosaic Virus ◽  
Raman Optical Activity ◽  
Satellite Tobacco Mosaic Virus ◽  
Chain Conformations

A vibrational Raman optical activity (ROA) study of a range of different structural types of virus exemplified by filamentous bacteriophage fd, tobacco mosaic virus, satellite tobacco mosaic virus, bacteriophage MS2 and cowpea mosaic virus has revealed that, on account of its sensitivity to chirality, ROA is an incisive probe of their aqueous solution structures at the molecular level. Protein ROA bands are especially prominent from which, as we have shown by comparison with the ROA spectra of proteins with known structures and by using a pattern recognition program, the folds of the major coat protein subunits may be deduced. Information about amino acid side-chain conformations, exemplified here by the determination of the sign and magnitude of the torsion angle χ2,1 for tryptophan in fd, may also sometimes be obtained. By subtracting the ROA spectrum of the empty protein capsid (top component) of cowpea mosaic virus from those of the intact middle and bottom-upper components separated by means of a caesium chloride density gradient, the ROA spectrum of the viral RNA was obtained, which revealed that the RNA takes up an A-type single-stranded helical conformation and that the RNA conformations in the middle and bottom-upper components are very similar. This information is not available from the X-ray crystal structure of cowpea mosaic virus since no nucleic acid is visible.

Structural characterization of proteins and viruses using Raman optical activity

2004 ◽  
Vol 35 (1-2) ◽  
pp. 87-92 ◽  
Author(s):  
Ewan W Blanch ◽  
Iain H McColl ◽  
Lutz Hecht ◽  
Kurt Nielsen ◽  
Laurence D Barron
Keyword(s):  
Optical Activity ◽  
Structural Characterization ◽  
Raman Optical Activity

scholarly journals Recognition of the true and false resonance Raman optical activity

2021 ◽  
Author(s):  
Malgorzata Baranska ◽  
Ewa Machalska ◽  
Grzegorz Zajac ◽  
Aleksandra J. Wierzba ◽  
Josef Kapitán ◽  
...  
Keyword(s):  
Optical Activity ◽  
Resonance Raman ◽  
Raman Optical Activity

scholarly journals Recognition of the true and false resonance Raman optical activity

2021 ◽  
Author(s):  
Malgorzata Baranska ◽  
Ewa Machalska ◽  
Grzegorz Zajac ◽  
Aleksandra J. Wierzba ◽  
Josef Kapitán ◽  
...  
Keyword(s):  
Optical Activity ◽  
Resonance Raman ◽  
Raman Optical Activity

Vibrational Raman Optical Activity of α-Lactalbumin: Comparison with Lysozyme, and Evidence for Native Tertiary Folds in Molten Globule States

1995 ◽  
Vol 254 (4) ◽  
pp. 747-760 ◽  
Author(s):  
Gary Wilson ◽  
Steven J. Ford ◽  
Alan Cooper ◽  
Lutz Hecht ◽  
Zai Q. Wen ◽  
...  
Keyword(s):  
Optical Activity ◽  
Molten Globule ◽  
Raman Optical Activity
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