Net Charge and Electrophoretic Mobility of Lysozyme Charge Ladders in Solutions of Nonionic Surfactant

Szymański, Jan; Poboży, Ewa; Trojanowicz, Marek; Wilk, Andrzej; Garstecki, Piotr; Hołyst, Robert

doi:10.1021/jp067511d

Cited by 15 publications

(16 citation statements)

References 33 publications

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“…Next (in Section 4) we discuss the influence of temperature on the motion in complex liquids. We also discuss the influence of in- 55 terparticle interactions on motion in the complex liquids. The influence of the depletion interactions on motion of a probe particle and its relation to the anomalous diffusion model is described in Section 5.…”

Section: Accepted Manuscriptmentioning

confidence: 99%

“…Before Kohli's work, Holyst et al [29] had also observed lengthscale dependence of the transport properties of complex liquids. Holyst et al [29] performed fluorescence correlation Szymanski et al [55] used the protein charge ladder method [57], where a set of lysozyme regioisomers differing in charge but not in size were dragged through a solution under an external electric field. In both works [29,55] the authors interpreted 135 their data in terms of the effective viscosity, η eff , experienced by the probe in motion; cf.…”

Section: The Modelmentioning

confidence: 99%

“…They also used capillary electrophoresis to monitor the electrophoretic mobility of the same proteins in polymer matrices as well as in micellar matrices[55] composed130 of rigid elongated micelles of non-ionic surfactant C 12 E 6[56].…”

mentioning

confidence: 99%

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Motion of nanoprobes in complex liquids within the framework of the length-scale dependent viscosity model

Kalwarczyk

Sozański

Ochab-Marcinek

et al. 2015

Advances in Colloid and Interface Science

118

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Section: Accepted Manuscriptmentioning

confidence: 99%

Section: The Modelmentioning

confidence: 99%

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Motion of nanoprobes in complex liquids within the framework of the length-scale dependent viscosity model

Kalwarczyk

Sozański

Ochab-Marcinek

et al. 2015

Advances in Colloid and Interface Science

118

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“…In ( b ), the data of the diamonds and dotted diamonds are collected from ( 39 ), and the crossed diamonds from ( 43 ). In ( c ), the data of the triangles are collected from ( 10 ), crossed diamonds from ( 39 ), square and dotted squares from ( 85 ), and the others from ( 41 ). …”

Section: Resultsmentioning

confidence: 99%

The Investigation of Protein Diffusion via H-Cell Microfluidics

Silva

Opstal

et al. 2019

Biophysical Journal

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In this study, we developed a microfluidics method, using a so-called H-cell microfluidics device, for the determination of protein diffusion coefficients at different concentrations, pHs, ionic strengths, and solvent viscosities. Protein transfer takes place in the H-cell channels between two laminarly flowing streams with each containing a different initial protein concentration. The protein diffusion coefficients are calculated based on the measured protein mass transfer, the channel dimensions, and the contact time between the two streams. The diffusion rates of lysozyme, cytochrome c, myoglobin, ovalbumin, bovine serum albumin, and etanercept were investigated. The accuracy of the presented methodology was demonstrated by comparing the measured diffusion coefficients with literature values measured under similar solvent conditions using other techniques. At low pH and ionic strength, the measured lysozyme diffusion coefficient increased with the protein concentration gradient, suggesting stronger and more frequent intermolecular interactions. At comparable concentration gradients, the measured lysozyme diffusion coefficient decreased drastically as a function of increasing ionic strength (from zero onwards) and increasing medium viscosity. Additionally, a particle tracing numerical simulation was performed to achieve a better understanding of the macromolecular displacement in the H-cell microchannels. It was found that particle transfer between the two channels tends to speed up at low ionic strength and high concentration gradient. This confirms the corresponding experimental observation of protein diffusion measured via the H-cell microfluidics.

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“…[8][9][10][11][12] Further, a new technical approach has been attempted in FCS for increasing the information obtained by the cross-correlation or fluorescence resonance energy transfer (FRET) techniques. [13][14][15] A confocal optical configuration has been adopted for observing most of FCS (see the review by Cognet et al).…”

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confidence: 99%

Optical Parameter Dependence of Fluorescence Correlation Spectrometry without Using Magnification Tools

2007

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Ever since Gösch et al. 1 applied fluorescence correlation spectrometry (FCS) to a microchannel flow system, this technique has attracted attention in various fields, including nano-and life-sciences, such as the flow system of fluorescent particles, 2 quantum dots, 3-5 DNA-fluorescent probe assemblies, 6,7 protein molecules, and living cell systems. [8][9][10][11][12] Further, a new technical approach has been attempted in FCS for increasing the information obtained by the cross-correlation or fluorescence resonance energy transfer (FRET) techniques. [13][14][15] A confocal optical configuration has been adopted for observing most of FCS (see the review by Cognet et al.).11 Recently, a numerical treatment or nonstandard method has been proposed by Culbertson et al. 16 However, the object dynamics vary with the flow and free Brownian motion; in some cases, calibration of the fluorescent particle size might be required.In the present note, in particular, the limitation in determining the empirical relationship between the pinhole diameter and the fluorescent particles size is investigated: we have shown that nanosize measurement is possible without any optical magnification. As a practical application, the microalgal size was measured with the present system. Experimental ReagentsAll the fluorescent particle standards were obtained from Polyscience Inc. (Fluoresbrite, Microsphere, POL series). The particles used were latex particles, whose surfaces were modified by fluorophores: the particles were stably suspended in aqueous media. We confirmed that the standard shows the maximum emission at 410 nm for an excitation wavelength of 325 nm. FCS measurement systemThe optical configuration was the same as that used for the ordinary fluorometry. Standard particles in an ordinary synthetic quartz cuvette used in fluorometry were driven by an ordinary cubic stirrer (GL Science, Type SRS 111A; with a stirring rod of Type TC-10) at a rate of 200 rpm. The excitation was performed by a He-Cd laser at 325 nm (Kinmon Koha Co. Ltd., Model IK-3251RF, 15 mW). The emission from the cuvette was directly detected by a photon counter (Hamamatsu, Model C8855) through a pinhole by employing 350-nm highpass and 410-nm (or 650-nm) band-pass filters (purchased from Edmund Optics). The diameter of the laser beam was about 0.7 mm. Therefore, observation volume can be calculated as about 0.4 × 10 -6 A ml (A = diameter (μm) of the pinhole used). The signal was processed by a real-time correlator (ALV-multiple tau digital real correlator 5000/60XO, ALV-GmbH, Germany) and transferred to a Windows XP computer to which the photon counting signal was also simultaneously transferred for display. Pinholes were purchased from Sigma Koki Co. In the present optical configuration, no tools were used for the magnification of the fluorescent images, i.e., a pinhole was set just in front of a photon counting detector near the sample cuvette. Cultivation of microalgaeSynechocystis sp. PCC 6803 and Chlorella kessleri C-531, a single-cell freshwater algae, ...

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Net Charge and Electrophoretic Mobility of Lysozyme Charge Ladders in Solutions of Nonionic Surfactant

Cited by 15 publications

References 33 publications

Motion of nanoprobes in complex liquids within the framework of the length-scale dependent viscosity model

Motion of nanoprobes in complex liquids within the framework of the length-scale dependent viscosity model

The Investigation of Protein Diffusion via H-Cell Microfluidics

Optical Parameter Dependence of Fluorescence Correlation Spectrometry without Using Magnification Tools

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