Biomedical subjects

Sheng-Jun Wang

Publications and source records attributed to Sheng-Jun Wang.

3 recordsLinked to original sources

PubMed2006

Effects of degree distribution in mutual synchronization of neural networks.

We study the effects of the degree distribution in mutual synchronization of two-layer neural networks. We carry out three coupling strategies: large-large coupling, random coupling, and small-small coupling. By computer simulations and analytical methods, we find that couplings between nodes with large degree play an important role in the synchronization. For large-large coupling, less couplings are needed for inducing synchronization for both random and scale-free networks. For random coupling, cutting couplings between nodes with large degree is very efficient for preventing neural systems from synchronization, especially when subnetworks are scale free.

Action Potentials↗

PubMed2006

Evolutionary prisoner's dilemma game with dynamic preferential selection.

We study a modified prisoner's dilemma game taking place on two-dimensional disordered square lattices. The players are pure strategists and can either cooperate or defect with their immediate neighbors. In the generations each player updates its strategy by following one of the neighboring strategies with a probability dependent on the payoff difference. The neighbor selection obeys a dynamic preferential rule, i.e., the more frequently a neighbor's strategy was adopted by the focal player in the previous rounds, the larger probability it will be chosen to refer to in the subsequent rounds. It is found that cooperation is substantially promoted due to this simple selection mechanism. Corresponding analysis is provided by the investigation of the distribution of the players' impact weights, persistence, and correlation function.

Journal Article↗

PubMed2005

[High level expression of PNGase F in Escherichia coli and its bioactivities].

In order to obtain active recombinant PNGase F in Escherichia coli, a prokaryotic expression vector pET28a/PNGase F was constructed. Amplification of PNGase F was obtained using PCR technique employing suitable primers designed according to the PNGase F gene sequence from Flavobacterium nmeningosepticum. The expression of PNGase F gene in LB medium or M9 medium led to the formation of inclusion body and soluble protein, respectively. The refolding of the denatured inclusion body was successful by gradual dilution. Further purification of the refolded protein and soluble crude extract from M9 medium with Ni2+ -NTA argarose resulted a 90% purified PNGase F. The purified protein catalyzed the complete and intact cleavage of N-linked oligosaccharides from various glycoproteins. The efficiency of this cleavage was affected by the substrate status in the reaction system. In summary, we have developed an enzyme production system where PNGase F was over-expressed in recombinant E. coli. This system can provide more than 15 mg/L purified active PNGase F. This purified active PNGase F can be used as tools in analyzing the oligosaccharide structure.

Bacterial Proteins↗