Monitoring of small conformational changes by high-precision measurements of hydrodynamic radius with 2-focus fluorescence correlation spectroscopy (2fFCS)

2007 ◽  
Author(s):  
Thomas Dertinger ◽  
Iris von der Hocht ◽  
Ingo Gregor ◽  
Konstantin Komolov ◽  
Karl-Wilhelm Koch ◽  
...  
Keyword(s):  
High Precision ◽  
Conformational Changes ◽  
Fluorescence Correlation Spectroscopy ◽  
Hydrodynamic Radius ◽  
Correlation Spectroscopy ◽  
Precision Measurements ◽  
Fluorescence Correlation

scholarly journals Characterization of protein adsorption onto FePt nanoparticles using dual-focus fluorescence correlation spectroscopy

2011 ◽  
Vol 2 ◽  
pp. 374-383 ◽  
Author(s):  
Pauline Maffre ◽  
Karin Nienhaus ◽  
Faheem Amin ◽  
Wolfgang J Parak ◽  
G Ulrich Nienhaus
Keyword(s):  
Fluorescence Correlation Spectroscopy ◽  
Hydrodynamic Radius ◽  
Serum Proteins ◽  
Correlation Spectroscopy ◽  
Fept Nanoparticles ◽  
Absolute Increase ◽  
Fluorescence Correlation ◽  
X Ray Crystallography ◽  
Blood Serum Proteins ◽  
Equilibrium Dissociation

Using dual-focus fluorescence correlation spectroscopy, we have analyzed the adsorption of three human blood serum proteins, namely serum albumin, apolipoprotein A-I and apolipoprotein E4, onto polymer-coated, fluorescently labeled FePt nanoparticles (~12 nm diameter) carrying negatively charged carboxyl groups on their surface. For all three proteins, a step-wise increase in hydrodynamic radius with protein concentration was observed, strongly suggesting the formation of protein monolayers that enclose the nanoparticles. Consistent with this interpretation, the absolute increase in hydrodynamic radius can be correlated with the molecular shapes of the proteins known from X-ray crystallography and solution experiments, indicating that the proteins bind on the nanoparticles in specific orientations. The equilibrium dissociation coefficients, measuring the affinity of the proteins to the nanoparticles, were observed to differ by almost four orders of magnitude. These variations can be understood in terms of the electrostatic properties of the proteins. From structure-based calculations of the surface potentials, positively charged patches of different extents can be revealed, through which the proteins interact electrostatically with the negatively charged nanoparticle surfaces.

Measurement of the Hydrodynamic Radius of Quantum Dots by Fluorescence Correlation Spectroscopy Excluding Blinking

2015 ◽  
Vol 119 (11) ◽  
pp. 4294-4299 ◽  
Author(s):  
A. A. de Thomaz ◽  
D. B. Almeida ◽  
V. B. Pelegati ◽  
H. F. Carvalho ◽  
C. L. Cesar
Keyword(s):  
Quantum Dots ◽  
Fluorescence Correlation Spectroscopy ◽  
Hydrodynamic Radius ◽  
Correlation Spectroscopy ◽  
Fluorescence Correlation

scholarly journals Using Fluorescence Correlation Spectroscopy to Study Conformational Changes in Denatured Proteins

2008 ◽  
Vol 94 (12) ◽  
pp. 4819-4827 ◽  
Author(s):  
Eilon Sherman ◽  
Anna Itkin ◽  
Yosef Yehuda Kuttner ◽  
Elizabeth Rhoades ◽  
Dan Amir ◽  
...  
Keyword(s):  
Conformational Changes ◽  
Fluorescence Correlation Spectroscopy ◽  
Correlation Spectroscopy ◽  
Fluorescence Correlation ◽  
Denatured Proteins

Conformational Changes and Aggregation of Alginic Acid as Determined By Fluorescence Correlation Spectroscopy

2007 ◽  
Vol 8 (1) ◽  
pp. 106-112 ◽  
Author(s):  
Fabrice Avaltroni ◽  
Marianne Seijo ◽  
Serge Ulrich ◽  
Serge Stoll ◽  
Kevin J. Wilkinson
Keyword(s):  
Conformational Changes ◽  
Fluorescence Correlation Spectroscopy ◽  
Alginic Acid ◽  
Correlation Spectroscopy ◽  
Fluorescence Correlation
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