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Analysis of the structure of the KRAS(G48A) mutant predicted altered interactions with other proteins.
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Such pattern is robust to alterations of the model parameters and simulated failures predict altered spatio-temporal patterns that mimic those described for several mutants.
Similarly, the L270M mutant is predicted to alter ligand specificity from cholesterol-binding to phospholipid-binding.
Using a genetic screen based on the inability to propagate the yeast [ PSI+] prion, we have identified 13 new Sse1 mutants that are predicted to alter chaperone function through a variety of different mechanisms.
The size of LPS synthesized in the deletion mutants was compared to wild-type strain U112, a strain that synthesizes a LPS without the core and O-antigen (ΔkdtA), two strains that synthesize a LPS lacking the O-antigen (ΔwbtA, wzx), and hypercytoxic transposon mutant htrB, which is predicted to alter the acylation of lipid A [26].
The most common RB1CC1 mutant, T10, greatly altered its predicted 3'UTR RNA secondary structure (Figure 3).
Below, translation of the disrupted locus in the mutants predicts a 33.6 kDa polypeptide.
The four mutants isolated in the SBD domain are predicted to alter either Sse1 interaction with cytosolic Hsp70 (E554K, G616D, see Figure S3), substrate binding (S440L), or protein−protein interactions (E504K) (Table 5 and Supplemental Information).
The most common RTF1 mutant, T9, altered both free energy and predicted RNA structure (data not shown).
Of the two approaches, 203 and 183 mutations were predicted to alter the target compartments of mutant proteins, affecting 105 and 92 proteins, respectively.
Furthermore, use of mutants of L22 which have lost the capacity to bind RNA would be predicted to alter telomerase activity as well as potentially impact the nucleolar localization of hTR.
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