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Since the PolD1 and PolE mutations affect the intrinsic proofreading activity, the observed mutational patterns could reflect the initial error signatures of the polymerases.
This is an indication that a high number of somatic mutations affect the cell function.
So those same sort of mutations affect the way people respond to pollutants as well.
Thus, it is possible that the mutations affect the conformational dynamics of the transporter in the non-native lipid environment.
Understanding how gene-level mutations affect the binding affinity of protein protein interactions is a key issue of protein engineering.
Understanding how pre-mRNA splicing is controlled will be important since at least 40% of the known human and mouse disease gene mutations affect the splicing process.
We plan to investigate how external conditions in the medium, i.e. temperature, denaturant concentration, etc., or point-directed mutations, affect the shape of the potential energy function.
The model helps us to understand how mutations affect the folding kinetics of WW domains, and captures also negative Φ-values that have been difficult to interpret.
Both energy calculation and geometric parameterization were used to interpret the simulated structures and predict how the mutations affect the dimer stability.
We hypothesize that these mutations affect the biomechanical properties of myosin, such as increasing its intrinsic force and/or its duty ratio and therefore the ensemble force of the sarcomere.
It will be interesting to test whether these mutations affect the catalytic activity of USP33 in future studies.
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