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Proteomics technology aims to map the protein landscapes of biological samples, and it can be applied to a variety of samples, including cells, tissues, and body fluids.
Polyacrylamide gel electrophoresis was used to map the protein profiles of the various cell lines.
First, it is not trivial to map the protein identifiers of the same sequence in both databases.
Radioligand labeling was performed to map the protein expression patterns of functional human and mouse AVPR1A receptors, and the resulting ligand-binding patterns in transgenic mice demonstrated that the human AVPR1A protein was expressed at high levels in a pattern profoundly divergent from that of the murine AVPR1A protein.
Despite this plethora of interesting chromatin proteins linked to interbands, their very cytological mapping is not accurate enough, as it is quite challenging to reliably map the protein localization signal to a fine structure of an interband, at least at the resolution level of light microscopy.
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We have also determined the interactions between these factors and several ribosomal proteins with known binding sites in order to map the protein-protein networks onto the structure of the ribosome.
With ChIP-Seq it is common to map the protein-DNA interactions to regions as small as about 300 bp.
ChIP followed by high-throughput sequencing (ChIP-Seq) has been developed to map the protein-DNA interactions at a genome-wide level [ 5, 6].
In another approach, Exonerate was used to map the proteins from all four genomes on intergenic sequences.
To perform such an analysis, we map the proteins contained in each pathway to their 'biological process', defined by the Gene Ontology (GO) [ 38].
Mapping the protein folding landscape is of central importance to understanding the mechanism of protein folding.
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