Sentence examples for interacting site for from inspiring English sources

The C-terminal domain of CEP135 contains an interacting site for its two binding partners, the 50 kDa dynactin complex subunit (p50) and C-Nap1.

Peptide array experiments identified the C-terminal 58 residues of the IC3 (IC3-C58) as the major interacting site for S100B.

Furthermore, they suggest that the major interacting site for the PIH-N domain of PIH1D1 (and budding yeast Pih1) is a short DpSDD motif that encompasses the only amino acids conserved between TEL2 orthologs from humans to yeast.

A large area comprising residues K241-S288 (A6-D5) from the IC3 exhibited very little observable fluorescence for both apo- or Ca2+-S100B Ca2+-S100Bg thindicatingof IC3 is nothismajoregionracting site fof S100B.

The deletions ΔSL1 (Δ7–34) or ΔSL3 (Δ246 255, Δ246–255) did not reduce eEF1A1 binding to the 3′UTR significantly, whereas the deletions in stem-loop 2 (Δ151 158–93, Δ151–158) abolished eEF1A1 binding, indicating that this region was the primary interacting site for eEF1A1.

The crystal structure of PIH-N domain fragment bound to the phosphorylated TEL2 peptide suggests that the major interacting site for the PIH-N domain is a short conserved DpS491DD motif, previously described as a CK2 phosphorylation site (Ahn et al., 2013, Horejsí et al., 2010).

Briefly, we randomly permutated calculated z-score data for every chromosome 100 times, and chose interacting sites with a false discovery rate (FDR) ≤ 5% or FDR ≤ 20% as positively interacting sites for inter-chromosomal or intra-chromosomal interactions.

These sensors contained single hydrogen-bond functional groups, which acted as interacting sites for fluoride ion.

This provides an important means for the prediction of the interacting sites on protein with the ligand molecules.

Significant effort has been made in looking for such correlations between the substitution processes at interacting sites.

If function type is used as an additional constraint, prediction accuracy usually increases, and is particularly good for enzymes, DNA-interacting sites, and oligomeric interfaces.