SPR analysis shows that NBD1 ΔF508 interacts more tightly than NBD1 wt with the α-subunit of CK2 and that CFTR peptides which are able to trigger NBD1 phosphorylation by CK2 holoenzyme also perturb the interaction between the α- and the β-subunits of CK2.
In the case of the E. coli clamp loader, the A subunit interacts more tightly with the clamp than do any of the other subunits [ 73]; it binds through a helix and loop that insert snugly into a hydrophobic pocket, accompanied by specific hydrogen bonds and ions pairs between the A subunit and clamp [ 32].
We also noted a significant overexpression of genes with GATA2 cofactor PU.1 motifs in their regulatory regions (p value NES = 2.06) in GATA2 biallelic vs. monoallelic samples, in support of a recent finding that p.Thr354Met mutants bind and interact with PU.1 more tightly than WT, thus leading to sequestration of PU.1 from its normal cellular functions.
The acetyl group is removed by one of the HDAC enzymes during deacetylation, allowing histones to interact with DNA more tightly to form compacted nucleosome assemblies, which can effectively silence gene transcription.
Polyamination of the H3 N-terminal tail increases its positive charge and its propensity to more tightly interact with negatively charged deoxyribonucleic acid (DNA), and hence participate in facultative heterochromatin formation.
The MDM2 aptamer (SuperTIP) interacted ∼ 2-fold more tightly with MDM2 than the free linear peptide (12.1 peptide), while the eIF4E aptamer elongation initiation factor 4GI-SG interacted ∼ 5-fold less strongly than the free linear peptide (elongation initiation factor 4GI).
We rephrased the sentence in question and now write: "The only notable deviation from the FG-binding pattern was observed with MtNup188, which was relatively inefficiently eluted with 1M NaCl from Nup100 1-310) and Nup100 1-610), suggesting that MtNup188 either interacts with these FG-repeat regions more tightly than ScKap95 or that these interactions are more hydrophobic in nature".
The only notable deviation from the FG-binding pattern was observed with MtNup188, which was relatively inefficiently eluted with 1M NaCl from Nup100(1 310) and Nup100(1 610), suggesting that MtNup188 either interacts with these FG-repeat regions more tightly than ScKap95 or that these interactions are more hydrophobic in nature.
These ridge modes are usually more tightly confined and hence interact weakly with side-wall roughness.
Based on muscle type differences described above it is predicted that flight but not climbing behavior will be more tightly linked to the interacting tRNA-synthase mutations.
