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Furthermore, the highly positively charged interface, mainly formed by α4 helix, is proposed to be responsible for nucleotide binding.
Finite-volume/multigrid methods are presented for solving incompressible heat flow problems with an unknown melt/solid interface, mainly in solidification applications, using primitive variables on collocated grids.
At high STE content (2%), STE dominated the formation of interface mainly by the preferential adsorption of STE molecules, as evidenced by the results of interfacial properties and surface protein load of emulsions.
A thorough study of the electronic structure reveals that the N-terminated interface is the polar covalent bond, and the Ti-terminated interface mainly shows the metallic covalent interaction.
An adaptive finite volume method is presented for solving incompressible heat flow problems with an unknown melt/solid interface, mainly in solidification applications, using primitive variables on a fixed collocated grid.
Currently, it may not be the optimal interface, mainly because of the high data rates required.
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It is also revealed that the optimal design considering interface behavior may exhibit tension/compression non-symmetric topology, in which material interfaces mainly undergo compression.
The strength and deformation of surrounding rocks with maturely developed interfaces mainly depend on the mechanical properties of the interfaces.
The catalytic sites were located at the three α β interfaces, mainly on the β-subunits.
Later, the first crystal structure of bovine mitochondrial F1-ATPase revealed by Walker and colleagues showed that the α and β subunits are arranged alternately, forming a ring, while the central γ subunit forms the central shaft deeply penetrating into the ring's central hole, and that the catalytic sites of ATP synthesis and hydrolysis are located at the α β interfaces, mainly on the β subunits.
The observed hydrophobic interactions at the IL-1α/SL1067 interface are mainly edge-to-face π interactions, exemplified by the base of dG1, which protrudes into a small hydrophobic pocket on the IL-1α surface.
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