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Lower hinge mutations caused large reductions in binding whereas modification of residues 327, 330 and 331 had less dramatic effects.
In order to overcome this limitation, we investigated whether the modification of residues significantly displaced upon the original mutation is an effective way to reduce protein aggregation in mammalian cells.
The electrochemical modification of residues in proteins [1] and other bioactive molecules offers the production of novel proteins, enzymes and other bioactive species, in comparison with traditional methodologies such as protein engineering and the use of chemical reagents.
The modification of residues outside of the RNP has the potential to alter the interactions between the RRM and an RNA [ 5].
The data revealed six modified residues, listed in Table 2. Of note, three of these, K145, K183, and K204, are located in the proposed DNA-binding domain of XPA, and two, K63 and K67, are known sites of acetylation that reduces XPA's interaction with replication protein A. Modification of residues within the XPA DNA-binding domain has the potential to affect DNA-binding activity.
Similar(55)
Modification of residue 113 with pyrene destabilized the wildtype illustrated by a broad loss of excimer (Figure 5C, dotted line).
Loss of modification of residue U1191 in the H31 loop was recently reported to inhibit site D cleavage (Liang et al, 2009), suggesting that this may influence the binding or activity of Rio2.
Moreover, presentation of this tyrosinase peptide by HLA-A*0201 HLA-A*0201he posttrequiresonal modificathen of residue 371Asn to Asposttranslationalchanismodificationofably inefficient in the TYresiduen polypeptide.
The concept of integrated biorefinery is then applied to an ethanol producing facility and a flow sheet of the main catalytic routes to promote modifications of residues is proposed.
This could argue in favour of proposed activation mechanisms that are based on modifications of residues by nitrosylation in the catalytic region rather than extensive conformational changes [32].
Variable modifications were set to GlyGly modification of lysine residues, oxidation of methionine residues, and pyroglutamate formation of N-terminal glutamine residues.
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