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Any mutation that causes a charge change (e.g., D407N and D408N) results in loss of transport activity (Guan and Nakae 2001; Middlemiss and Poole 2004).
We noted that all the ψRACK sequences within each PKC isozyme have at least one non-homologous amino acid difference from their corresponding RACK that constitutes a charge change.
Two of these supernumerary residues are basic (Lys159, His175) while none is acidic, so that the mutant protein is likely to have a charge change mirroring or exceeding that of the proteins encoded by the distantly related b alleles of S. invicta (which have a unique Lys151 replacement).
Such a charge change in a conserved region of an ion transporter could have a large effect on protein function.
The FAD2-1B presentutatinn PIesent in PI 283327 represents a charge change for the substituted amino acid since proline is nonpolar while arginine is basic.
The fact that this polymorphism at amino acid 129 without a charge change partially determines which brain regions are targeted indicates that factors other than charge differences are driving selective vulnerability.
Similar(52)
Due to the presence of a metal on the polymer surface, the effect of a surface charge change plays an important role accumulation of electrons [27, 46].
P-EIM measures electrical impedance optically with high spatial resolution by converting a surface charge change to a surface plasmon resonance (SPR) image intensity change, and the signal is not scaled to the mass of the analyte.
The final rP11-4 sample remained a mixture of peptide alone and that with an additional homoserine lactone derived from the intervening Met residue cleavage, resulting in a net charge change from −2 to −1 at pH 7.4.
Non-conservative mutations were those that resulted in a change in charge, change in hydrophobicity, change in side chain size, and inclusion/replacement of proline or glycine.
The present comparative evolutionary analysis implies that since the gene duplication event, the electric charges of the two PGI isoforms changed steadily through many charge-changing substitutions in both directions of charge change; only a few charged amino acid sites were specific to PGI-1 or PGI-2.
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