Time-Resolved Fluorescence and Essential Dynamics Study on the Structural Heterogeneity of p53DBD Bound to the Anticancer p28 Peptide

2020 ◽  
Vol 124 (44) ◽  
pp. 9820-9828
Author(s):  
Anna Rita Bizzarri ◽  
Salvatore Cannistraro
2020 ◽  
Vol 11 (24) ◽  
pp. 6121-6133 ◽  
Author(s):  
Ryan Clark ◽  
Mohd A. Nawawi ◽  
Ana Dobre ◽  
David Pugh ◽  
Qingshan Liu ◽  
...  

The behaviour of two molecular rotors have been studied in various ionic liquids. Time resolved fluorescence shows a complex relationship between the bulk viscosity of the ionic liquid and microstructure of solvent around each molecular rotor.


2016 ◽  
Vol 291 (33) ◽  
pp. 17382-17393 ◽  
Author(s):  
Pierre Volz ◽  
Nils Krause ◽  
Jens Balke ◽  
Constantin Schneider ◽  
Maria Walter ◽  
...  

A variant of the cation channel channelrhodopsin-2 from Chlamydomonas reinhardtii (CrChR2) was selectively labeled at position Cys-79 at the end of the first cytoplasmic loop and the beginning of transmembrane helix B with the fluorescent dye fluorescein (acetamidofluorescein). We utilized (i) time-resolved fluorescence anisotropy experiments to monitor the structural dynamics at the cytoplasmic surface close to the inner gate in the dark and after illumination in the open channel state and (ii) time-resolved fluorescence quenching experiments to observe the solvent accessibility of helix B at pH 6.0 and 7.4. The light-induced increase in final anisotropy for acetamidofluorescein bound to the channel variant with a prolonged conducting state clearly shows that the formation of the open channel state is associated with a large conformational change at the cytoplasmic surface, consistent with an outward tilt of helix B. Furthermore, results from solute accessibility studies of the cytoplasmic end of helix B suggest a pH-dependent structural heterogeneity that appears below pH 7. At pH 7.4 conformational homogeneity was observed, whereas at pH 6.0 two protein fractions exist, including one in which residue 79 is buried. This inaccessible fraction amounts to 66% in nanodiscs and 82% in micelles. Knowledge about pH-dependent structural heterogeneity may be important for CrChR2 applications in optogenetics.


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Andreea Lorena Mateescu ◽  
Nicolae-Bogdan Mincu ◽  
Silvana Vasilca ◽  
Roxana Apetrei ◽  
Diana Stan ◽  
...  

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.


2014 ◽  
Vol 289 (39) ◽  
pp. 26817-26828 ◽  
Author(s):  
Christoph Röthlein ◽  
Markus S. Miettinen ◽  
Tejas Borwankar ◽  
Jörg Bürger ◽  
Thorsten Mielke ◽  
...  

Sign in / Sign up

Export Citation Format

Share Document