| 초록 |
Nuclear pore complex is one of the largest protein complexes, consisting of dozens of different nucleoporins, and acts as a selective gateway for nucleo-cytoplasmic transports. However, the in vivo three-dimensional structures of nucleoporins inside the nuclear pore and their relations to the selective gating functions remain elusive. Motivated by the natively unfolded nature of nucleoporins with FG repeats, we consider a nucleoporin as a polymer brush grafted to the inside of a cylinder. Based on exact evaluation of a partition function and a scaling theory, we obtain the phase diagram of equilibrium conformations. We also find the conformational phase transitions between different network connectivity, which play a crucial role in the highly selective gating function of NPC. This result is supported by extensive Monte Carlo simulation, which implies the cooperative nature of hydrophobic interaction among FG residues leads to drastic functional changes in nuclear transports. |
