Sentence examples for loop binding from inspiring English sources

In IRS2, the kinase regulatory loop binding domain has been identified while IRS-4 has PTB and PH domains, which binds to INSR.

To determine a cut-off that may define a discrete population of mRNAs associated with DRBP76, we applied a percentile rank transformation, which was used in the analysis of stem loop binding protein (SLBP) and tris-tetra-proline RIP-Chip targets [29], [30].

The involvement of finger loop binding to rhodopsin was expected, but the evidence of the arrestin 160 loop contacting rhodopsin was not.

An additional motif that contributes to receptor recruitment, the kinase regulatory loop binding (KRLB) domain, has been identified only in IRS-2 (Fig. 1)[ 22, 24].

Each ankyrin repeat consists of 33 amino acids, which form a β-turn followed by two anti-parallel α-helices and a loop binding to the β-turn of the next ankyrin repeat [ 18, 19].

The first binding event (K1) is typical of an interaction via end stacking [ 29, 40, 42], while the second binding event (K2) is probably due to the interaction via groove or external loop binding [ 41, 42].

Stem-loop binding protein (SLBP) directly binds the stem-loop of histone mRNAs and is necessary for correct processing of histone pre-mRNAs [20], and is absolutely required for processing Drosophila pre-mRNAs in vitro [21].

The histone RNA-binding protein HBP/SLBP (hairpin-binding protein/stem-loop binding protein), an essential regulator of histone gene expression, binds to the conserved hairpin structure located in the 3′UTR (untranslated region) of histone mRNA and participates in histone pre-mRNA processing, translation and histone mRNA degradation.

A second explanation is that this binding is weak and does not survive gel resolution in binding shift assays; (3) hnRNP H was seen to directly bind to the stem-loop IDX-rasISS1 that involves a dsRNA stem-loop structure (Figure 2E, lanes 4 9); and (4) p68 regulates hnRNP H-stem-loop binding since p68 reduces this interaction (Figure 2E and 2F).

One mutation of particular importance for clinical investigations is the multi-resistant substitution T315I, resulting in an amino acid change within the p-loop binding site.

We suggest that introducing more electronegative groups into such hydrophobic compounds may provide more specific interactions in a closed-loop binding pocket proposed here.