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To test the functional relevance of our SLiM conservation calculation, we analyzed reported SH2 binding sites in 11 highly-studied RTKs (with greater than 30 interaction partners, according to Hprd), including EGFR, IR, KIT, PDGFRB, IGF-IR, VEGFR2, ERBB2, FGFR1, HGFR, RET and TKR-A.
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In a first set of calculations, we analyzed in each protomer separately, including all ionizable side-chains in the calculation.
We also note that in our calculations, we analyze only the isotropic part of CR intensity.
In the first approximation made to obtain the circuit model that will allow for the calculation of GICs, we analyzed the 400-kV network only.
To test how reproducible this calculation may work we analyzed a mixture of 48 recombinant proteins distributed over an abundance range of 6 orders of magnitude.
We analyzed the pKa calculations in terms of a measure termed BIPS (binary protonation states) recently introduced by us.
We analyzed the π-calculation problem on an 8-worker cluster to be split up into 10, 50, 100, 500, and 1000 uniform tasks respectively.
We analyze this complementarity using calculations, z-scan measurements on water and oils, and THG-FWM imaging of cell divisions in live zebrafish embryos.
The scaling of various parts of a HARES calculation is analyzed and compared to that of plane-wave based methods.
Then, the relevant deviations in the forward calculation are analyzed, and an inversion model is proposed to revise the model parameters.
Both the procedures used to couple the different calculation domains analyzed by time domain models and to interface fluid dynamic and linear acoustic models have been developed.
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