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This process frees the long molecules from close association with one another, allowing them to move independently.
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The time-resolved mode allows to discriminate the signal arising from molecules in close proximity from the background fluorescence of excess amounts of unbound fluorescent marker and from cell autofluorescence.
Although crystallographic symmetry places identical hydrophobic patches from neighboring protein molecules in close proximity, there are no intermolecular van der Waals contacts between hydrophobic residues of different proteins and the protein in solution is a monomer.
Relative to the DE loop, residue 95 is located on the opposite pole of the β2-m tertiary structure; in the crystal packing, however, the two regions, from spatially neighbouring molecules, fall close to each other, hence the observed flexibility of the C-terminal region may affect the conformational flexibility of the DE loop.
All sites are also accessible to protons, either by channels or from water molecules close to the metal sites.
The number of lipid layers corresponds to the number of lipid molecules from a protein to the closest system edge so that this option can be used to quickly estimate the total number of lipid molecules.
The signal amplification results from an increased electromagnetic field experienced by the molecules in close proximity to the metal surface.
Therefore, the dye molecules are close enough to enable Förster resonance energy transfer (FRET) from the protonated to the deprotonated form.
In this arrangement, some carbonyl/nitrous groups from different molecules are brought close to each other favouring the splitting of the energetic levels.
The mechanism of cellular toxicity from irradiation is the result of direct DNA damage secondary to free radical formation and its damage to molecules in close proximity.
Consequently, one acceptor molecule absorbs the energy harvested of several donor molecules in close proximity.
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