scholarly journals An infrared sensor analysing label-free the secondary structure of the Abeta peptide in presence of complex fluids

2015 ◽  
Vol 9 (3) ◽  
pp. 224-234 ◽  
Author(s):  
Andreas Nabers ◽  
Julian Ollesch ◽  
Jonas Schartner ◽  
Carsten Kötting ◽  
Just Genius ◽  
...  
2017 ◽  
Vol 2 (2) ◽  
pp. 1700072 ◽  
Author(s):  
Marcello Berto ◽  
Chiara Diacci ◽  
Roberta D'Agata ◽  
Marcello Pinti ◽  
Elena Bianchini ◽  
...  

Author(s):  
John P. Robinson ◽  
J. David Puett

Much work has been reported on the chemical, physical and morphological properties of urinary Tamm-Horsfall glycoprotein (THG). Although it was once reported that cystic fibrotic (CF) individuals had a defective THG, more recent data indicate that THG and CF-THG are similar if not identical.No studies on the conformational aspects have been reported on this glycoprotein using circular dichroism (CD). We examined the secondary structure of THG and derivatives under various conditions and have correlated these results with quaternary structure using electron microscopy.THG was prepared from normal adult males and CF-THG from a 16-year old CF female by the method of Tamm and Horsfall. CF female by the method of Tamm and Horsfall.


2020 ◽  
Author(s):  
Nikolas Hundt

Abstract Single-molecule imaging has mostly been restricted to the use of fluorescence labelling as a contrast mechanism due to its superior ability to visualise molecules of interest on top of an overwhelming background of other molecules. Recently, interferometric scattering (iSCAT) microscopy has demonstrated the detection and imaging of single biomolecules based on light scattering without the need for fluorescent labels. Significant improvements in measurement sensitivity combined with a dependence of scattering signal on object size have led to the development of mass photometry, a technique that measures the mass of individual molecules and thereby determines mass distributions of biomolecule samples in solution. The experimental simplicity of mass photometry makes it a powerful tool to analyse biomolecular equilibria quantitatively with low sample consumption within minutes. When used for label-free imaging of reconstituted or cellular systems, the strict size-dependence of the iSCAT signal enables quantitative measurements of processes at size scales reaching from single-molecule observations during complex assembly up to mesoscopic dynamics of cellular components and extracellular protrusions. In this review, I would like to introduce the principles of this emerging imaging technology and discuss examples that show how mass-sensitive iSCAT can be used as a strong complement to other routine techniques in biochemistry.


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