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Few techniques are suited to probe the structure and dynamics of molecular complexes at the mesoscale level (∼100-1000 nm).
Whether this is also true of the gas giant's interior has been unknown1,2, limiting our ability to probe the structure and composition of the planet3,4.
We are pushing the envelope of ultrafast mid-IR spectroscopic methods to probe the structure and dynamics at surface and in bulk systems, and further applying them to a series of novel systems.
Advances in RNA nanotechnology will depend on the ability to manipulate, probe the structure and engineer the function of RNA with high precision.
Here, we probe the structure and folding transition of Itrap and compare them to those of M. Hydroxyl radical and dimethyl sulfate footprinting show that both Itrap and M are extensively structured and crudely resemble the native RNA.
In this review, it will be described how we have used Zn2+-binding sites as a tool to probe the structure and function of Na+/Cl−-coupled biogenic amine transporters with specific focus on the human DAT (hDAT).
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Here we probe the structures and peptide-binding activities of variants that affect the BRCA1 BRCT phosphopeptide-binding groove.
But, beyond that, I have the great privilege of scrutinizing the very mechanism of his novels, of probing the structure and supporting tissue.
Using synchrotron X-ray diffraction (XRD), the Richard Robinson group (Cornell University) directly probed the structure and reaction kinetics of lead sulfide (PbS) nanocrystals (NCs) undergoing cationic exchange to cadmium sulfide (CdS).
Neutron scattering and diffraction methods are of utmost importance for probing the structure and dynamics of condensed matter at an atomic, molecular and mesoscopic level.
Our study demonstrates that careful compressional experiments with powder diffraction can be a useful means for probing the structure and behavior of the surface layer in nanocrystalline materials.
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