Sentence examples for binding when mutated to from inspiring English sources

Most of the residues that were found to abolish actin binding when mutated to alanine are strongly conserved.

Recently, systematic mutagenesis of charged surface-exposed residues of yeast coronin revealed a patch of residues extending over the top and one side of the β-propeller that abolished actin binding when mutated to alanine.

The three V2 residues that conferred the strongest binding to CH58-UA when mutated to Ala were Leu179 (a ~ 6.1-fold increase in the SPR binding response compared to wild-type peptide), Ile181 (a ~ 3.9-fold increase in the same), and Val182 (a ~ 3.4-fold increase in the same).

We previously identified a conserved arginine residue (Arg) within the β-propeller domain of Coro1B, which when mutated to aspartate (R30D) abolished F-actin binding [ 22].

Non-hotspots are the residues that when mutated to alanine causes a change in the binding energy by less than 0.4 kcal/mol.

When mutated to alanine, histidines 323 and 449 within the ligand-binding domain of PPARγ failed to abolish binding to and activation by 1-O-octadecenyl glycerophosphate but completely abolished the binding of and activation induced by rosiglitazone.

Hotspots are the interface residues that contribute maximally toward the stability of the complex, and when mutated to alanine, they impart an appreciable decrease in binding strength (difference of 2 kcal/mol or more in the binding energy).

Several residues lining the putative binding acyl chain binding site were mutated to purturb substrate binding.

The mutations in the DNA bases reduced the value of the negative energies of binding (maximum value for ΔΔG = 42Kcal/mol for F1 when GCG mutated to GGG, and ΔΔG = 22 kcal/mol for F2, the loss in total energy of binding originated in the loss in electrostatic energies upon mutation (r =.98).

All residues from the predicted binding-region were mutated to Ala.

Amino-acid-sequence alignments suggest that Tah1 is most similar to the TPR2b domain of Hop (Hsp-organizing protein) which when mutated reduces binding to both Hsp90 and Hsp70.