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-amino acids are used in racemic crystallography to create centrosymmetric crystals, which (depending on the protein) may allow for easier and more robust protein structure determination.
One of the newly engineered split intein bearing C-terminal 15 residues showed more robust protein trans-splicing activity than naturally occurring split DnaE inteins in a foreign context.
However, we have recently discovered that DnaE intein from Nostoc punctiforme (Npu) has more robust protein trans-splicing activity than that of SspDnaE intein and is also more tolerant of amino acid replacements at the C-terminal splicing junction [24].
A recently established label-free strategy [16], [17] has been shown to offer a more robust protein identification and quantitation, easy automation and large-scale analysis with greater efficiency as compared to conventional two dimensional electrophoresis (2-DE) approaches [18], [19], [20], [21].
However, when cellobiose was used as the poor cellulase inducer for QM9414, QM-Mbgl2 showed significantly more robust protein production than did QM9414 (Fig. 8b).
The reason for higher level protein production by Ao38 cells is unclear although it may result from either more robust protein synthetic machinery, more efficient protein transport and processing, or some combination of these factors.
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Alternatively, it may be the case that only more robust protein-protein associations survive during the fractionation procedure of the PSD, although the selective process is still consistent among samples.
We have demonstrated that neutral evolution favors more mutationally robust proteins when the evolving population is highly polymorphic.
Thus, irrespective of the experimental method employed, we found that (1) ePPID is a better predictor of protein evolutionary rate than PPID, (2) ePPID is a more robust predictor of protein evolutionary rate than PPID, and (3) the contribution of ePPID to protein evolutionary rate is statistically independent of expression level.
However, temporal instability of beef heart LDH indicates the need for further protein engineering prior to development of a more robust lactate-sensing protein.
However, to detect more subtle differences between land plant proteomes, more robust methods using protein structure and molecular dynamic simulations [ 59] may be needed to resolve more subtle protein adaptations to thermal stress.
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