New Possibilities of Investigating Nucleic Acids and Nucleoproteins in Aqueous Solutions by Infrared Spectroscopy

Nature ◽  
1972 ◽  
Vol 235 (5338) ◽  
pp. 386-388 ◽  
Author(s):  
M. SHIE ◽  
I. G. KHARITONENKOV ◽  
T. I. TIKHONENKO ◽  
Yu. N. CHIRGADZE
Keyword(s):  
Infrared Spectroscopy ◽  
Nucleic Acids ◽  
Aqueous Solutions

Preparation and Characterization of Heparin-Immobilized Poly(Ether Urethanes)

2011 ◽  
Vol 393-395 ◽  
pp. 236-239
Author(s):  
Li Ming Lian ◽  
Bing Leng ◽  
Xiao Hua Ma
Keyword(s):  
Contact Angle ◽  
Fourier Transform ◽  
Infrared Spectroscopy ◽  
Aqueous Solutions ◽  
Fourier Transform Infrared Spectroscopy ◽  
Toluidine Blue ◽  
Water Contact ◽  
The Fourier Transform ◽  
Hydrolysis Of

Heparin (Hep)-immobilized poly(ether urethanes) (PU) was prepared by a unique preparation procedure. Firstly, the poly(ether urethanes)(PU) containing diester groups in the side chains were synthesized. Then, PU was dispersed in aqueous solutions and immobilized with heparin after the hydrolysis of diester groups and carboxylation. The Fourier transform infrared spectroscopy (FTIR) and water contact angle (WCA) were used to characterize the heparin-bonded PU. The amount of heparin grafted on the PU was determined to be 0.57wt.% by the toluidine blue method. The heparin-immobilized PU could release just 12% of the immobilized heparin in the early 10 hours of the 70 hours immobilized heparin stability test.

scholarly journals Infrared spectroscopy of heparin-cation complexes

1987 ◽  
Vol 244 (1) ◽  
pp. 143-149 ◽  
Author(s):  
D Grant ◽  
W F Long ◽  
F B Williamson
Keyword(s):  
Infrared Spectroscopy ◽  
Aqueous Solutions ◽  
Fundamental Region ◽  
Ion Binding ◽  
Cation Effects ◽  
Cation Complex ◽  
Cation Complexes ◽  
Electrostatic Theory

Hydrated and partially hydrated films and aqueous solutions of heparin, heparans and N-desulphated preparations of these polymers were studied by near- and fundamental-region-i.r. spectroscopy in the presence of a range of countercations. The results suggest that ion binding is not explicable solely in terms of simple electrostatic theory, and that specific cation effects, and the hydration pattern of the polymer-cation complex need to be taken into account.

scholarly journals Hydration of Ions in Aqueous Solutions Studied by Infrared Spectroscopy. II. Application.

1984 ◽  
Vol 38a ◽  
pp. 613-618 ◽  
Author(s):  
Olof Kristiansson ◽  
Anders Eriksson ◽  
Jan Lindgren ◽  
Masunobu Maeda ◽  
Hitoshi Ohtaki
Keyword(s):  
Infrared Spectroscopy ◽  
Aqueous Solutions

Temperature-dependent near-infrared spectroscopy for studying the interactions in protein aqueous solutions

NIR news ◽  
2019 ◽  
Vol 30 (5-6) ◽  
pp. 15-17
Author(s):  
Mian Wang ◽  
Xiaoyu Cui ◽  
Wensheng Cai ◽  
Xueguang Shao
Keyword(s):  
Infrared Spectroscopy ◽  
Aqueous Solutions ◽  
Near Infrared Spectroscopy ◽  
Structural Changes ◽  
Near Infrared ◽  
Molten Globule ◽  
Hydration Shell ◽  
Protein S ◽  
Temperature Dependent ◽  
Water Species

Temperature-dependent near-infrared spectroscopy has been developed for studying quantitative and structural analysis, as well as the molecular interactions. Taking the advantage of the temperature effect on hydrogen bonding, the technique has shown its potential in analyzing the interactions in aqueous solutions. In our recent studies, the structural changes in homo-oligopeptides K5 (penta-lysine), D5 (penta-aspartic acid), and protein (ovalbumin) aqueous solutions were studied by temperature-dependent near-infrared spectroscopy. The thermodynamics and their interaction with water were analyzed with the help of the chemometric methods including continuous wavelet transform, independent component analysis, two-dimensional (2D) correlation analysis, and Gaussian fitting. The results show that the oligopeptide in aqueous solution improves the thermal stability of the water species, and K5 has stronger interaction with water than D5. In the gelation of ovalbumin, the change of the water species with two hydrogen bonds (S2) follows the same phases as the protein. S2 maintains the stability of the protein in native and molten globule states, and the weakening of the hydrogen bond in S2 by high temperature results in the destruction of the hydration shell and makes the ovalbumin clusters form a gel structure.

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