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These were based on high-throughput interaction detection methods, such as i) yeast two-hybrid systems [19], [20], ii) protein complex purification techniques using mass spectrometry [21], [22], iii) correlated messenger RNA expression profiles [23], [24], iv) genetic interaction data [25], [26], and v) "in silico" interaction predictions derived from gene context analysis.
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The two-hybrid (Y2H) screens (Ito et al., 2001; Rual et al., 2005; Stelzl et al., 2005; Uetz et al., 2000) and complex purification detection techniques using mass spectrometry (Gavin et al., 2002, 2006; Ho et al., 2002) are the two most popular approaches thus far applied successfully on a large scale.
Although a protein developed to be a biosimilar will have a nominal primary amino acid sequence the same as the reference product, the manufacturer of the biosimilar has to develop its own production methodology, having no access to the complex production and purification techniques used for the reference product.
We extracted only data derived by affinity purification techniques leading to 1,060 complexes with 6,136 annotated proteins.
The technique is illustrated on a complex purification process where published multifactorial data had been collected for a critical wastewater paradigm and thus may be used to test the benchmark solution.
Mass spectrometry combined with affinity purification techniques has evolved as a prime tool for the in-depth study of distinct protein complexes and protein protein interactions.
Nevertheless, differentiation and purification techniques are improving with each study.
However, high-purity purification techniques still have to be developed.
Too many different protein and enzyme purification techniques have been reported, especially, chromatographic techniques.
This method also presents a facile route to high-yield MWCNTs without complex purification processes.
Nevertheless, a viable solution to this drawback has been successfully proven via kinase affinity purification techniques.
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