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In the central helix, the central arginine R23 is of particular importance in binding to bacterial membranes or DNA.
As previously mentioned, the main feature of J-domain proteins is a highly conserved HPD motif, which may indicate its importance in binding to DnaK.
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To assess indirectly the importance of key residues in binding to VPg and/or m7GTP, an extensive range of point mutants in eIF4E was tested for their ability to complement PSbMV multiplication in resistant pea tissues and for complementation of protein translation, and hence growth, in an eIF4E-defective yeast strain conditionally dependent upon ectopic expression of eIF4E.
They suggest that the low agonist activity of ANA10 may reflect the importance of residue 10 in binding to the Kiss1r, but that this requires experimental confirmation.
They reported that the frequency of arginine expression among murine anti-dsDNA antibodies was highest at position 100, and they postulate that the importance of this residue in binding to dsDNA lies in its position at the centre of the VH CDR3 loop in the structure of the antigen combining site [ 52].
Structural studies of a number of transcriptional regulators have demonstrated the importance of amphipathic α-helices in binding to transcriptional coregulators.
Mutations at H221, D223, H277 and R287 completely abolished enzymes activities, supporting their importance in binding ferrous iron and 2-oxoglutarate.
The study identified PKI-179 interacting residues of both the proteins and their importance in binding was ranked by the loss in accessible surface area, number of molecular interactions of the residue, and consistent appearance of the residue in (un binding simulation analysis.
The importance in binding of the conserved glutamine and of the two flanking residues was demonstrated by mutational studies [37].
The high conservation of these three aspartic acid residues reflects their importance in binding Mg2+ as a cofactor.
Structural, biophysical and mutagenesis data demonstrate the importance of nucleotide binding to STRADα in influencing STRADα's ability to interact with its biological partners (LKB1 and MO25), as well as the ability of STRADα to activate the LKB1 tumour suppressor kinase [ 28,27 ].
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