Because of the binding of HIV-1 to contaminating leukocytes (Fig. 3A), the question arose whether the apparent binding of HIV-1 to non-hemolyzed cells actually consisted of binding to the small number of contaminating CD4 cells.
Streptomycin inhibits translation by binding to the small subunit of the bacterial ribosome and has thereby no effect on ribosomal folding activity in vitro, while chloramphenicol binds to the domain V of the 23S rRNA of the large subunit of the bacterial ribosome thus also inhibiting ribosomal protein folding activity in vitro.
GalP activity was assessed by monitoring binding to the small molecule inhibitor forskolin.
This probably reflects differences in HPLF binding to the smaller, more defined, detergent micelles which is presumably much tighter than binding to the larger, more irregular lipid bodies.
A primary reason was hypothesized to be due to steric interference in anti- CD4 antibody binding to the smaller sized lyophilized control cells.
These proteins selectively recognize autophagic cargo and mediate its engulfment into autophagosomes by binding to the small ubiquitin-like modifiers that belong to the Atg8/LC3 family.
Although the bead control successfully identified target proteins, it also produced a list of moderate to highly abundant proteins with weak but differential binding to the small molecule.
The human TAR RNA-binding protein, TRBP, was first identified and cloned based on its high affinity binding to the small hairpin trans-activation responsive (TAR) RNA of HIV-1.
This repression is relieved by RsmA binding to the small, noncoding regulatory RNA (sRNA) RsmB, instead of its target mRNAs [ 14].
This factor – IF2, eIF5B and aIF5B in bacteria, eukaryotes and archaea respectively – is required for promoting initiator tRNA binding to the small ribosomal subunit, and the recruitment of the large subunit in order for translation to begin [ 92, 93].
