Particle sizing by quasi-elastic light scattering

Finsy, Robert

doi:10.1016/0001-8686(94)80041-3

Cited by 286 publications

(238 citation statements)

References 203 publications

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“…The normalized ACFs, G(), were fitted using Equation 1 appropriate for scattering of non-interacting protein molecules of fixed size (49,50),…”

Section: Methodsmentioning

confidence: 99%

“…The hydrodynamic radius (R H ) of unassembled CA was then calculated from D 0 using the Stokes-Einstein relationship. For the icosahedral particle preparations, measurements were made on solutions with a total [CA] ϭ 47 M. Normalized ACFs were fitted with a generalization of Equation 2, appropriate when there are several non-interacting species of fixed size present in solution (49,50).…”

Section: Methodsmentioning

confidence: 99%

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Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles

Hyun¹,

Radjainia

Kingston

et al. 2010

Journal of Biological Chemistry

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In a mature and infectious retroviral particle, the capsid protein (CA) forms a shell surrounding the genomic RNA and the replicative machinery of the virus. The irregular nature of this capsid shell precludes direct atomic resolution structural analysis. CA hexamers and pentamers are the fundamental building blocks of the capsid, however the pentameric state, in particular, remains poorly characterized. We have developed an efficient in vitro protocol for studying the assembly of Rous sarcoma virus (RSV) CA that involves mild acidification and produces structures modeling the authentic viral capsid. These structures include regular spherical particles with T ‫؍‬ 1 icosahedral symmetry, built from CA pentamers alone. These particles were subject to cryoelectron microscopy (cryo-EM) and image processing, and a pseudo-atomic model of the icosahedron was created by docking atomic structures of the constituent CA domains into the cryo-EM-derived three-dimensional density map. The N-terminal domain (NTD) of CA forms pentameric turrets, which decorate the surface of the icosahedron, while the C-terminal domain (CTD) of CA is positioned underneath, linking the pentamers. Biophysical analysis of the icosahedral particle preparation reveals that CA monomers and icosahedra are the only detectable species and that these exist in reversible equilibrium at pH 5. These same acidic conditions are known to promote formation of a RSV CA CTD dimer, present within the icosahedral particle, which facilitates capsid assembly. The results are consistent with a model in which RSV CA assembly is a nucleation-limited process driven by very weak protein-protein interactions.

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“…The normalized ACFs, G(), were fitted using Equation 1 appropriate for scattering of non-interacting protein molecules of fixed size (49,50),…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles

Hyun¹,

Radjainia

Kingston

et al. 2010

Journal of Biological Chemistry

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“…The particle diffusive motion in liquid is size dependent, and a larger particle has a slower motion as compared to a smaller particle. This brownian motion can be investigated by irradiating the sample with a coherent laser and studying the intensity fluctuations of the scattered light (Finsy, 1994).…”

Section: Nanoparticle Characterizationmentioning

confidence: 99%

“…This implies that the temperature must be constant during the measurement and the viscosity of the sample solvent must be known. It should be noted that the formula shown above (Equation 1) is valid only for non-interacting spherically shaped particles, i.e experimental data are fitted to a model assuming spherical particles (Finsy, 1994). Figure 1 shows five different functions representing the typical information retrieved in DLS in the actual measurement and by using algorithms.…”

Section: Nanoparticle Characterizationmentioning

confidence: 99%

Two-Dimensional Gel Electrophoresis and Mass Spectrometry in Studies of Nanoparticle-Protein Interactions

Karlsson¹,

Ljunggren²,

Ahrén³

et al. 2012

Gel Electrophoresis - Advanced Techniques

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“…[1][2][3][4] Pioneering work goes back to Gustav Mie a century ago, who reported the assignment of light scattering patterns of colloidal metal particles. [5] It is well-known that Mie scattering is accompanied by a typical intense forwardscattering lobe for x >> 1, where x is the Mie size parameter (x = πD/λ).…”

Section: Introductionmentioning

confidence: 99%

Elastic light scattering from free sub-micron particles in the soft X-ray regime

et al. 2008

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We report the first experimental results on angle-resolved elastic light scattering in the soft X-ray regime, where free sub-micron particles in the size regime between 150 and 250 nm are studied in the gas phase by using a continuous particle beam. Two different types of studies are reported: (i) Angle-resolved elastic light scattering experiments provide specific information on the scattering patterns in the regime of element-selective inner-shell excitation near the Si 2p-edge (80-150 eV). In addition to intense forward scattering, we observe distinct features in the angle-resolved scattering patterns. These are modelled by using Mie theory as well as a model that includes contributions from diffuse and specular reflection. The results are primarily attributed to scattering from soft X-rays in the surface layer. (ii) Spectroscopic experiments are reported, where the photon detector is placed at a given scattering angle while scanning the photon energy near the Si 2p-absorption edge. These results are also analyzed by a Mie model, yielding accurate information of the size distribution.

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Particle sizing by quasi-elastic light scattering

Cited by 286 publications

References 203 publications

Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles

Proton-driven Assembly of the Rous Sarcoma Virus Capsid Protein Results in the Formation of Icosahedral Particles

Two-Dimensional Gel Electrophoresis and Mass Spectrometry in Studies of Nanoparticle-Protein Interactions

Elastic light scattering from free sub-micron particles in the soft X-ray regime

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