Temperature Dependent Near Infrared Spectroscopy for Understanding the Hydrogen Bonding of Amines

2018 ◽  
Vol 76 (4) ◽  
pp. 298 ◽  
Author(s):  
Xuewei Zhu ◽  
Xiaoyu Cui ◽  
Wensheng Cai ◽  
Xueguang Shao
Keyword(s):  
Hydrogen Bonding ◽  
Infrared Spectroscopy ◽  
Near Infrared Spectroscopy ◽  
Near Infrared ◽  
Temperature Dependent

Understanding the function of water during the gelation of globular proteins by temperature-dependent near infrared spectroscopy

2018 ◽  
Vol 20 (30) ◽  
pp. 20132-20140 ◽  
Author(s):  
Li Ma ◽  
Xiaoyu Cui ◽  
Wensheng Cai ◽  
Xueguang Shao
Keyword(s):  
Infrared Spectroscopy ◽  
Hydrogen Bonds ◽  
Near Infrared Spectroscopy ◽  
Near Infrared ◽  
Globular Proteins ◽  
Temperature Dependent

Water with two hydrogen bonds plays an important role in the gelation of globular proteins.

scholarly journals Temperature-Dependent Near-Infrared Spectroscopy for Sensitive Detection of Glucose

2020 ◽  
Vol 78 (2) ◽  
pp. 125
Author(s):  
Mingyuan Wang ◽  
Xiaoyu Cui ◽  
Wensheng Cai ◽  
Xueguang Shao
Keyword(s):  
Infrared Spectroscopy ◽  
Near Infrared Spectroscopy ◽  
Near Infrared ◽  
Sensitive Detection ◽  
Temperature Dependent

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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