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Molecular Architecture of the Transport Channel of the Nuclear Pore Complex

The Rockefeller University

 

  

Summary: Nobel laureate G. Blobel and colleagues at The Rockefeller University have determined the crystal structure of the nucleoporin interacting domains, Nup54·Nup58 and Nup62·Nup54. These nucleoporins are thought to modulate the ring diameter of receptors and transport activity of the central channel for mammalian nucleocytoplasmic transport. Wyatt Technology’s DAWN HELEOS, DynaPro Titan, and Optilab rEX were utilized to determine the molar masses for Nup58-2 protomer and Nup54-4.
CELL
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S. Solmaz, R Chauhan, G. Blobel, Ivo Melčák , “Molecular Architecture of the Transport Channel of the Nuclear Pore Complex," Cell 147, pp 590-602 (2011). DOI: [10.1016/j.cell.2011.09.034]

 

 
 
Wyatt Technology is the recognized leader in light scattering instrumentation and software for determining the absolute molar mass, size, charge and interactions of macromolecules and nanoparticles in solution. These tools include: in-line multi-angle static light scattering, high-throughput dynamic light scattering, differential refractometry, electrophoretic mobility, differential viscosity, field flow fractionation and automated composition gradients.