The rates of heme loss from the heme-binding proteins were thus conversely related to how tightly the proteins might bind to heme.
Deregulation of RNA-binding proteins is thus emerging as a prominent source of complex transcriptomic diversity that can serve as a platform for the selection of metastatic traits during tumor progression.
The canonically structured mammalian "KRAB A" domain interacts with a universal cofactor, KAP1, which recruits histone deacetylase complexes to the ZNF-binding sites, and KRAB-ZNF proteins are thus thought to act as potent transcriptional repressors (Margolin et al. 1994; Pengue et al. 1994; Witzgall et al. 1994; Vissing et al. 1995).
The capacity to bind to a variety of potential binding sites on the surfaces of many proteins is thus embedded in the polypeptide construct.
The immobilized preparation from direct binding of overexpressed fusion protein was thus useful for practical applications since it possessed high enzymatic activity and allowed the purification step to be eliminated.
Unfortunately, vitamin D binding protein was not routinely measured, and thus we are unable to reanalyze our data to answer the very interesting question of whether an association of bioavailable 25(OH D concentrations with clinically important outcomes is present.
All three SYT-binding proteins are known epigenetic controllers, thus these interactions are thought to regulate the coactivating function of SYT.
In both Gb3 and GM3, the apolar side of the central galactosyl group has a similar orientation to that in GalCer (Fig. 3a c); thus, GalCer-binding proteins are predicted to also bind to Gb3 and GM3 through CH π stacking.
Thus, choline-binding proteins are necessary for adherence of both high- and low-binding S. pneumoniae to epithelial cell surfaces.
The effect of biotin-binding on the protein stability of steroid-binding proteins was much smaller than in the case of wtAvd, thus showing decreased biotin affinity.
Through mRNA maturation, export, subcellular localization, stability, and degradation, RNAs are accompanied by RNA-binding proteins (RBPs) and are thus found as messenger ribonucleoproteins (mRNPs).
