Influence of mycosporine-like amino acids and gadusol on the rheology and Raman spectroscopy of polymer gels

Biorheology ◽  
2014 ◽  
Vol 51 (4-5) ◽  
pp. 315-328 ◽  
Author(s):  
Maira Gaspar Tosato ◽  
Dalila E. Orallo ◽  
M. Sandra Churio ◽  
Airton A. Martin ◽  
Claudio A. Telléz Soto ◽  
...  
Keyword(s):  
Amino Acids ◽  
Raman Spectroscopy ◽  
Polymer Gels

Infrared and Raman spectroscopy and DFT calculations of DL amino acids: Valine and lysine hydrochloride

2017 ◽  
Vol 1127 ◽  
pp. 419-426 ◽  
Author(s):  
F.M. Paiva ◽  
J.C. Batista ◽  
F.S.C. Rêgo ◽  
J.A. Lima ◽  
P.T.C. Freire ◽  
...  
Keyword(s):  
Amino Acids ◽  
Raman Spectroscopy ◽  
Dft Calculations ◽  
Infrared And Raman Spectroscopy

scholarly journals The Only N-H...O Hydrogen Bond - Two Ways to Build a Structure of Dimethylglycine

2014 ◽  
Vol 70 (a1) ◽  
pp. C550-C550
Author(s):  
Eugene Kapustin ◽  
Vasily Minkov ◽  
Elena Boldyreva
Keyword(s):  
Crystal Structure ◽  
Phase Transition ◽  
Amino Acids ◽  
Raman Spectroscopy ◽  
Single Crystal ◽  
Van Der Waals Interactions ◽  
X Ray Diffraction ◽  
Space Symmetry ◽  
Polarized Raman ◽  
Crystalline Amino Acids

Crystalline amino acids are considered to mimic important interactions in peptides, therefore the studies of the structure-forming factors in these systems attract much attention. N,N-dimethylglycine is an interesting model compound that was used to test the role of the N-H...O H-bonds in forming the head-to-tail chains – the main structural unit in the crystals of amino acids. It was hypothesized previously that additional side N-H...O H-bonds play an important role in forming the head-to-tail chains of amino acid zwitterions linked via N-H...O H-bonds between the charged -NH3 and -COO terminal groups. Twice methylated amino group of N,N-dimethylglycine is able to form only one N-H...O H-bond in the crystal structure, so that this hypothesis could be tested. There are two polymorphs of N,N-dimethylglycine, in which the zwitterions are packed in two different ways. In one polymorph (orthorhombic, Pbca) they form finite four member ring motifs not linked to each other via any H-bonds, but only by weak van der Waals interactions. However, in the second polymorph (monoclinic, P21/n) the zwitterions do form infinite head-to-tail chains though the N-H...O H-bond is the only one and is not assisted via any additional H-bonds. The effect of cooling on the two crystal structures was followed by single-crystal X-ray diffraction combined with polarized Raman spectroscopy of oriented single crystals, in order to compare the response of the N-H...O H-bonds to temperature variations. The crystal structure of the monoclinic polymorph compresses anisotropically on cooling, whereas that of the orthorhombic polymorph undergoes a reversible single-crystal to single-crystal phase transition at ~200 K accompanied by non-merohedral twinning, reducing the space symmetry to monoclinic (P21/b), and doubling the asymmetric unit from 2 to 4 molecules. This phase transition could not be detected by Raman spectroscopy and DSC because of the subtle related changes in intermolecular energies.

scholarly journals The Carbonate, Co3−·, in Solution Studied by Resonance Raman Spectroscopy

1999 ◽  
Vol 19 (1-4) ◽  
pp. 311-316 ◽  
Author(s):  
Susan M. Tavender ◽  
Steven A. Johnson ◽  
Daniel Balsom ◽  
Anthony W. Parker ◽  
Roger H. Bisby
Keyword(s):  
Amino Acids ◽  
Raman Spectroscopy ◽  
Group Theory ◽  
Free Radical ◽  
Resonance Raman Spectroscopy ◽  
Resonance Raman ◽  
Point Group ◽  
Biological Significance ◽  
Molecular Symmetry ◽  
Resonance Raman Spectra

The carbonate radical (Co3−·) is of biological significance acting as an intermediate in free radical-mediated damage and is capable of oxidising amino acids and proteins. In order to distinguish between the four possible structures of Co3−·, nanosecond timeresolved resonance Raman (TR3) experiments were undertaken. Photolysis of persulphate at 250 nm generated the So4−· radical which then oxidised sodium carbonate. Resonance Raman spectra of the resulting Co3−· radical were obtained using a probe wavelength of 620 nm. Point group theory calculations and interpretation of the TR3 spectra suggest that the radical has C2v molecular symmetry.

scholarly journals SERS study on myeloperoxidase and its immunocomplex: Identification of binding interactions

2010 ◽  
Vol 24 (3-4) ◽  
pp. 183-190
Author(s):  
Elisabeth S. Papazoglou ◽  
Sundar Babu ◽  
David R. Hansberry ◽  
Sakya Mohapatra ◽  
Chirag Patel
Keyword(s):  
Amino Acids ◽  
Raman Spectroscopy ◽  
Conformational Changes ◽  
Surface Enhanced Raman Spectroscopy ◽  
Biological Molecules ◽  
Sers Spectrum ◽  
Amino Acid Residues ◽  
Igg Antibodies ◽  
Surface Enhanced ◽  
Surface Enhanced Raman

Surface Enhanced Raman Spectroscopy (SERS) has demonstrated significant benefit in the identification of biological molecules. In this paper we have examined how to identify and differentiate the 150 kDa protein myeloperoxidase (MPO) from its corresponding antibody (Ab) and their immunocomplex through the use of SERS. The SERS signal of these biological molecules was enabled by 40 nm gold nanoparticles. The SERS spectra for both MPO and the Ab (an IgG molecule) demonstrated results consistent with previous published work on the Raman spectra of MPO and IgG antibodies. The immunocomplex SERS spectra showed peak shifts and intensity variations that could be attributed to conformational changes that occur during immunocomplex formation. Several key spectral areas have been identified which correspond to specific amino acids being shielded from undergoing resonance while new amino acid residues are made visible in the SERS spectrum of the immunocomplex and could be a result of conformational binding. These results indicate that SERS can be used to identify binding events and distinguish an immunocomplex from its individual components.

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