Time‐resolved fluorescence and hole‐burning line shapes of solvated molecules: Longitudinal dielectric relaxation and vibrational dynamics

1987 ◽  
Vol 87 (10) ◽  
pp. 5840-5857 ◽  
Author(s):  
Roger F. Loring ◽  
Yi Jing Yan ◽  
Shaul Mukamel
Keyword(s):  
Dielectric Relaxation ◽  
Hole Burning ◽  
Time Resolved Fluorescence ◽  
Vibrational Dynamics ◽  
Time Resolved ◽  
Line Shapes ◽  
Solvated Molecules

scholarly journals The influence of sugar–protein complexes on the thermostability of C-reactive protein (CRP)

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Andreea Lorena Mateescu ◽  
Nicolae-Bogdan Mincu ◽  
Silvana Vasilca ◽  
Roxana Apetrei ◽  
Diana Stan ◽  
...  
Keyword(s):  
Diagnostic Tests ◽  
Protein Complexes ◽  
C Reactive Protein ◽  
Time Resolved Fluorescence ◽  
Time Resolved ◽  
Reactive Protein ◽  
In Vitro Diagnostic ◽  
The Stability ◽  
Positive Controls

AbstractThe purpose of the present study was to evaluate de influence of protein–sugar complexation on the stability and functionality of C-reactive protein, after exposure to constant high temperatures, in order to develop highly stable positive controls for in-vitro diagnostic tests. C-reactive protein is a plasmatic protein used as a biomarker for the diagnosis of a series of health problems such as ulcerative colitis, cardiovascular diseases, metabolic syndrome, due to its essential role in the evolution of chronic inflammation. The sugar–protein interaction was investigated using steady state and time resolved fluorescence. The results revealed that there are more than two classes of tryptophan, with different degree of accessibility for the quencher molecule. Our study also revealed that sugar–protein complexes have superior thermostability, especially after gamma irradiation at 2 kGy, the protein being stable and functional even after 22 days exposure to 40 °C.

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