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Structure-based combinatorial protein engineering (SCOPE) is a homology-independent recombination method to create multiple crossover gene libraries by assembling defined combinations of structural elements ranging from single mutations to domains of protein structure.
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Levels of linkage disequilibrium (LD) and nucleotide divergence between inverted and standard chromosome arrangement change over time, and become reduced towards the middle of the inversion where multiple crossover and gene conversion are expected to be higher see [ 1], although this is not always the case (e.g., [ 18]).
Presented here is the development a semi-rational protein engineering approach that uses information from protein structure coupled with established DNA manipulation techniques to design and create multiple crossover libraries from non-homologous genes.
Multiple mechanisms have been postulated to explain the development of satellite repeats, including unequal crossover, gene conversion, satellite transposition, illegitimate recombination, and segmental duplication [ 2, 5, 16, 21, 28, 29].
Or perhaps a multiple crossover episode.
Dante has also appeared as a guest character in multiple crossover games.
In palliative care, single crossover trials have been published [ 30], but there are few multiple crossover formal SPTs [ 31].
Participants who fail to complete a single cycle of the multiple crossover phase will be replaced.
We used standard genetic crosses to measure the frequency of single and multiple crossover events.
In vitro recombination methods such as DNA shuffling are very flexible and can give hybrid genes with multiple crossovers; they have been used extensively to evolve proteins with improved and novel properties.
One caveat of the RD-PCR for the shuffling of fluorescence genes is the dominant finding of only one crossover per gene, while DNA shuffling resulted often in multiple crossovers.
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