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In particular, plasma-assisted chemical grafting methods enable surface functionalization of biomaterials providing covalent bonds between the substrate and the polymer monomers.
The most persistent hydrogen bonds between the substrate and the enzyme are those of the substrate with the carboxylate of Glu73 and the backbone amides of Leu51′ and Leu72, observed in >95% of the snapshots of the MD trajectory.
The building of an atomic model of the complex of EcDHNA and the substrate DHNP and the MD simulation of the complex show that some of the hydrogen bonds between the substrate and the enzyme are persistent, whereas others are transient.
The hydrogen bonds between the substrate DHNP and the enzyme EcDHNA suggested by the MD simulation are largely similar to those between the inhibitor NP and the enzyme EcDHNA in the crystal structure, indicating that the inhibitor NP is a good mimic of the substrate DHNP and the MD simulation indeed reflects the dynamics of the enzyme.
The MD simulation of the EcDHNA complex also shows that the substrate DHNP is anchored in the active site by four hydrogen bonds between the substrate (the groups at positions 2, 3, and 4) and the protein (backbone amides of Leu51′ and Leu72 and carboxylate of Glu73).
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The film also improved bonding between the substrate and the ceramic layer.
The results showed that good interfacial bonding between the substrate and coating was present before and after DTC.
A polarising H-bond between the substrate amine group and an Asp-Glu pair may facilitate oxidation.
The results showed that a good interfacial bonding between the substrate and the coating was present before and after DTC test.
Cladding is generally characterized by partial dilution of the substrate and hence formation of metallurgical bonding between the substrate and the deposits.
It was observed that the reaction proceeds via acylation of the active serine of BCL and demonstrating strong hydrogen bond between the substrate and histidine site.
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