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PLoS One. 2019 Jun 6;14(6):e0217897. doi: 10.1371/journal.pone.0217897. eCollection 2019.

Interactions of nuclear transport factors and surface-conjugated FG nucleoporins: Insights and limitations.

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Laboratory of Cellular and Structural Biology, the Rockefeller University, New York, NY, United States of America.
Department of Chemical and Biological Engineering and Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States of America.
Laboratory of Mass Spectrometry and Gaseous Chemistry, the Rockefeller University, New York, NY, United States of America.


Protein-protein interactions are central to biological processes. In vitro methods to examine protein-protein interactions are generally categorized into two classes: in-solution and surface-based methods. Here, using the multivalent interactions between nucleocytoplasmic transport factors and intrinsically disordered FG repeat containing nuclear pore complex proteins as a model system, we examined the utility of three surface-based methods: atomic force microscopy, quartz crystal microbalance with dissipation, and surface plasmon resonance. Although results were comparable to those of previous reports, the apparent effect of mass transport limitations was demonstrated. Additional experiments with a loss-of-interaction FG repeat mutant variant demonstrated that the binding events that take place on surfaces can be unexpectedly complex, suggesting particular care must be exercised in interpretation of such data.

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