Evolutionary origin of a calcium-dependent protease by fusion of genes for a thiol protease and a calcium-binding protein?

Calcium-dependent protease (calcium protease) is apparently involved in a variety of cellular processes. Here we have attempted to clarify the role and regulatory mechanism of calcium protease by analysing its structure. The complete primary structure of calcium protease (relative molecular mass (Mr) 80,000 (80K), 705 amino acids) was deduced from the nucleotide sequence of cloned complementary DNA. The protein contains four distinct domains, and we have observed a marked similarity between the second and fourth domains and the papain-like thiol proteases and calmodulin-like calcium-binding proteins, respectively. This finding suggests that calcium protease arose from the fusion of genes for proteins of completely different function and evolutionary origin. Further, it provides functional insight into cellular regulatory mechanisms mediated by Ca2+ through calcium-binding proteins.     

Molecular dynamics simulation of injection of polyethylene fluid in a variable cross-section nano-channel

Numerical simulation of injection of polyethylene fluid in a variable cross-section nano-channel was carried out using the molecular dynamics method.The effects of the nano-channel cross-section and the external force on the rheological behavior and structural properties of the polyethylene fluid were investigated.It was found that an absorbed layer appeared near the wall and the thickness of the absorbed layer increased with increasing cone angle of the nano-channel.The injection distance of the polyethylene fluid decreased with increasing cone angle and decreasing external force.In the nano-channel with cone angle 45°,polyethylene particles uniformly filled the whole channel and were stretched along the flow direction.Uniaxial stretching of particles was enhanced when the external force was strengthened,which facilitates injection of the polyethylene fluid into the nano-channel.