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In a laboratory in Boston, Dr. Higgins, a 40-year-old associate professor of microbiology and molecular genetics at Harvard Medical School, oversees graduate students tending samples of proteins drawn from infectious disease cells.
As summarized in [20], until now 16 different PseAAC modes have been used to represent the samples of proteins for predicting their attributes.
In order to perform a 2D-DIGE proteomic profiling, 18 independent samples of proteins were prepared from UVB-treated and non-treated cells considered at 16, 40 and 64 h (3 UVB-treated and 3 control samples at each time) after the eight exposures to UVB.
Duplicate samples of proteins from purified LDs were separated by AU-gel electrophoresis.
To reduce the concentration of imidazole in the samples of proteins, the eluates were subjected to a dialysis in phosphate buffer having a final concentration of 2.5 mM.
Complexes extracted from cells can be viewed as snapshot samples of proteins that have come together with adequate stability to be isolated.
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Protein concentrations were determined by spectrophotometry via a BCA protein assay kit, and 20 ug samples of protein were fractionated by electrophoresis in 5% stacking and 15% resolving acrylamide gels and transferred to PVDF filters (Immobilon-P Transfer Membrane).
Samples of protein were harvested following treatment using 2x Laemmli buffer.
Near optimal training can be achieved with only 1000 annotated sites, or roughly three samples of protein sequence alignments.
In order to detect these effects using samples of protein-coding sequences, we construct and examine three diagnostic statistics.
Control samples of protein alone, substrate alone, or protein and either nucleotide or nucleic acid were also measured; closed-state complexes were not detected in these cases.
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