Sentence examples for binding for normal from inspiring English sources

Applications of REFERs to oligomeric proteins began with hemoglobin (7,13) and were then applied, using αL analysis, to characterize the rate changes for conformational interconversions as a function of agonist binding for normal nicotinic acetylcholine receptors (nAChRs) (4) and a myasthenic mutant (14).

Moreover the program predicted a different pattern of substrate binding sites for normal and mutated protein: of the seven binding sites predicted for the normal SBEIIa-D, in SBEIIa-D V398I) SBEIIa-D V398Iere consixved and two new residues resulted involved in substrate binding.

This difference in average fold decrease did not meet standard criteria for significance (P = 0.07), and the decrease in Abf1 enrichment at memory effect targets such as RPN8 and CNB1 confirms that transcript levels remain high in spite of Abf1 dissociating from its binding site at genes (at least some) that depend on their Abf1 binding site for normal levels of transcription.

This implies that the enzyme was no longer flipping the base into the methyltransferase binding pocket [ 34], a process that contributes a significant amount of the binding energy for normal Type IIG recognition.

The TfRscFv-GAL4 targeted the protein-DNA complex to tumor cells and enhanced the transfection efficiencies in vitro, but it did not exhibit the binding activity for normal tissues.

EMSA analysis showed that in cells over-expressing the transcription factor MTF-1 there was an increase in binding for the normal MRE-containing probe compared to the mutant probe as indicated by the band intensity shift when compared to unlabelled probe (Figure 3A & B).

Scatchard analysis of the binding data obtained for normal thyroid parenchyma distant to the nodule area revealed heterogeneity of the [3H]iloprost sites exhibiting a high-affinity binding capacity (Bmax) of 613.2 +/- 130.4 fmol mg-1 membrane protein and a low-affinity binding capacity of 5.1 +/- 1.6 pmol mg-1 membrane protein.

This study reports the importance of the tightly balanced expression of the RNA-binding protein TIAR for normal embryonic development, thereby emphasizing the role of post-transcriptional regulations in early embryonic programming.

Murine models were used to demonstrate that the CD22 ligand binding domain is critical for normal B-cell survival.

Lgs/BCL9 proteins are adaptors between Armadillo/β-catenin and Pygo proteins [ 20, 30], and the interactions of Lgs with these binding partners are critical for normal development in flies [ 31, 32].

Furthermore, our data supports the hypothesis that appropriate regulation of RNA-binding proteins is critical for normal development and adult plasticity.