Elastic behaviors of protein-like chains are investigated by Pruned-Enriched-Rosenbluth method and modified orientation-dependent monomer-monomer interactions model. The protein-like chain is pulled away from the attr...Elastic behaviors of protein-like chains are investigated by Pruned-Enriched-Rosenbluth method and modified orientation-dependent monomer-monomer interactions model. The protein-like chain is pulled away from the attractive surface slowly with elastic force acting on it. Strong adsorption interaction and no adsorption interaction are both considered. We calculate the characteristic ratio and shape factor of protein-like chains in the process of elongation. The conformation change of the protein-like chain is well depicted. The shape of chain changes from “rod” to “sphere” at the beginning of elongation. Then, the shape changes from “sphere” to “rod”. In the end, the shape becomes a “sphere” as the chain leaves away from the surface. In the meantime, we discuss average Helmoholtz free energy per bond, average energy per bond, average adsorbed energy per bond, average α-helical energy per bond, average β-sheet energy per bond and average contact energy per bond. On the other hand, elastic force is also studied. It is found that elastic force has a long plateau during the tensile elongation when there exists adsorption interaction. This result is consistent with SMFS experiment of general polymers. Energy contribution to elastic force and contact energy contribution to elastic force are both discussed. These investigations can provide some insights into the elastic behaviors of adsorbed protein chains.展开更多
We study the translocation of a protein-like chain through a finite cylindrical channel using the pruned-enriched Rosenbluth method （PERM） and the modified orientation-dependent monomer-monomer interaction （ODI） m...We study the translocation of a protein-like chain through a finite cylindrical channel using the pruned-enriched Rosenbluth method （PERM） and the modified orientation-dependent monomer-monomer interaction （ODI） model. Attractive channels （εcp = -2.0, -1.0, -0.5）, repulsive chanaels （εcp： 0.5, 1.0, 2.0）, and a neutral channel （εcp =- 0） are discussed. The results of the chain dimension and the energy show that Z0 ： 1.0 is an important case to distinguish the types of the channels. For the strong attractive channel, more contacts form during the process of translocation. It is also found that an external force is needed to drive the chain outside of the channel with the strong attraction. While for the neutral, the repulsive, and the weak attractive channels, the translocation is spontaneous.展开更多
基金ACKNOWLEDGMENT This work was supported by the National Natural Science Foundation of China （No.20904047）.
文摘Elastic behaviors of protein-like chains are investigated by Pruned-Enriched-Rosenbluth method and modified orientation-dependent monomer-monomer interactions model. The protein-like chain is pulled away from the attractive surface slowly with elastic force acting on it. Strong adsorption interaction and no adsorption interaction are both considered. We calculate the characteristic ratio and shape factor of protein-like chains in the process of elongation. The conformation change of the protein-like chain is well depicted. The shape of chain changes from “rod” to “sphere” at the beginning of elongation. Then, the shape changes from “sphere” to “rod”. In the end, the shape becomes a “sphere” as the chain leaves away from the surface. In the meantime, we discuss average Helmoholtz free energy per bond, average energy per bond, average adsorbed energy per bond, average α-helical energy per bond, average β-sheet energy per bond and average contact energy per bond. On the other hand, elastic force is also studied. It is found that elastic force has a long plateau during the tensile elongation when there exists adsorption interaction. This result is consistent with SMFS experiment of general polymers. Energy contribution to elastic force and contact energy contribution to elastic force are both discussed. These investigations can provide some insights into the elastic behaviors of adsorbed protein chains.
基金Project supported by the National Natural Science Foundation of China （Grant No. 20904047）, the Science and Technology Planning Project of Zhejiang Province, China （Grant No. 20100022）, and the Natural Science Foundation of Zhejiang Province, China （Grant No. Y6110304）.
文摘We study the translocation of a protein-like chain through a finite cylindrical channel using the pruned-enriched Rosenbluth method （PERM） and the modified orientation-dependent monomer-monomer interaction （ODI） model. Attractive channels （εcp = -2.0, -1.0, -0.5）, repulsive chanaels （εcp： 0.5, 1.0, 2.0）, and a neutral channel （εcp =- 0） are discussed. The results of the chain dimension and the energy show that Z0 ： 1.0 is an important case to distinguish the types of the channels. For the strong attractive channel, more contacts form during the process of translocation. It is also found that an external force is needed to drive the chain outside of the channel with the strong attraction. While for the neutral, the repulsive, and the weak attractive channels, the translocation is spontaneous.
