Single-molecule transport across an individual biomimetic nuclear pore complex

2011 ◽  
Vol 6 (7) ◽  
pp. 433-438 ◽  
Author(s):  
Stefan W. Kowalczyk ◽  
Larisa Kapinos ◽  
Timothy R. Blosser ◽  
Tomás Magalhães ◽  
Pauline van Nies ◽  
...  
Keyword(s):  
Single Molecule ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
Molecule Transport

scholarly journals In Vitro Measurements of Single-Molecule Transport Across an Individual Biomimetic Nuclear Pore Complex

2011 ◽  
Vol 100 (3) ◽  
pp. 521a ◽  
Author(s):  
Cees Dekker ◽  
Stefan Kowalczyk ◽  
Larissa Kapinos ◽  
Roderick Y.M. Lim
Keyword(s):  
Single Molecule ◽  
Nuclear Pore Complex ◽  
Nuclear Pore ◽  
In Vitro Measurements ◽  
Molecule Transport

scholarly journals Physical modelling of multivalent interactions in the nuclear pore complex

2020 ◽  
Author(s):  
Luke K. Davis ◽  
Anđela Šarić ◽  
Bart W. Hoogenboom ◽  
Anton Zilman
Keyword(s):  
Experimental Data ◽  
Single Molecule ◽  
Nuclear Pore Complex ◽  
Intrinsically Disordered Proteins ◽  
Binding Kinetics ◽  
Disordered Proteins ◽  
Minor Role ◽  
Nuclear Pore ◽  
Minimal Models ◽  
Intrinsically Disordered

In the nuclear pore complex (NPC), intrinsically disordered proteins (FG Nups) along with their interactions with more globular proteins called nuclear transport receptors (NTRs) are vital to the selectivity of transport into and out of the cell nucleus. While such interactions can be modelled at different levels of coarse graining, in-vitro experimental data have been quantitatively described by minimal models that describe FG Nups as cohesive homogeneous polymers and NTRs as uniformly cohesive spheres, where the heterogeneous effects have been smeared out. By definition, these minimal models do not account for the explicit heterogeneities in FG Nup sequences, essentially a string of cohesive and non-cohesive polymer units, and at the NTR surface. Here, we develop computational and analytical models that do take into account such heterogeneity at a level of minimal complexity, and compare them to experimental data on single-molecule interactions between FG Nups and NTRs. Overall, we find that the heterogeneous nature of FG Nups and NTRs plays a minor role for their equilibrium binding properties, but is of significance when it comes to (un)binding kinetics. Using our models, we predict how binding equilibria and kinetics depend on the distribution of cohesive blocks in the FG Nup sequences and of the binding pockets at the NTR surface, with multivalency playing a key role. Finally, we observe that single-molecule binding kinetics has a rather minor influence on the diffusion of NTRs in polymer melts consisting of FG-Nup-like sequences.

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