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Results indicated higher binding of the yeast total RNA to the membrane in the presence of the RRM.
By use of in vivo chromatin immunoprecipitation (ChIP), lrs mutants have been shown to have reduced binding of the yeast silencing information regulatory (SIR) proteins at loci normally targeted for silencing.
Charge reversal mutations of the two basic residues in this conserved turn had earlier been found to abrogate binding of the yeast RACK1 ortholog (Asc1p) to the ribosome (vide supra).
Alternatively, the positively charged lysine residues might interact with pMMO or with negatively charged phospholipid headgroups at the periplasmic membrane surface, analogous to the lysine-mediated binding of the yeast copper chaperone for superoxide dismutase (CCS) to lipid bilayers.
Thus, a double charge reversal mutation (R38D K40E) in the RDK B-C turn of blade 1 almost fully ablates binding of the yeast protein (Asc1p) to the ribosome [ 79, 84].
The possible reason for the poor SSF performance with low inoculation OD could be that the yeast cell viability was inhibited by the solid's inhibitory effect due to the binding of the yeast cells to the fermentation solid residues [ 27, 28].
Similar(53)
NMR and isothermal titration calorimetry (ITC) studies of H3/H4 binding to the yeast histone chaperone RTT106 found that H3 K56ac) significantly enhanced binding to a double pleckstrin-homology (PH) domain, while fluorescence studies found that H3 K56ac) increases H3/H4 binding to the yeast histone chaperone CAF-1.
Because the site-specific lysine acetylation in histones, and the N- or C-terminal sequences of histones are conserved between yeast and human, we reasoned that knowledge of histone binding selectivity of the yeast BRDs can help understand the ligand binding selectivity of the human BRDs.
52 Briefly, the DNA binding domain of the yeast Gal4 transcription factor was fused in-frame to the N terminus of the ligand binding domains of human PPARα (amino acids 167 469), mouse PPARγ (amino acids 174 476) or human PPARδ (amino acids 139 442) receptors.
Iyer, V.R. et al. Genomic binding sites of the yeast cell-cycle transcription factors SBF and MBF.
Histone binding selectivity of the yeast BRDs was assayed by a dot blot assay.
More suggestions(15)
binding of the viral
binding of the initiator
binding of the peptide
binding of the myosin
binding of the action
binding of the anti-fibrinogen
binding of the karma
binding of the rabbit
binding of the radiolabel
binding of the protein
binding of the nation
binding of the p57T143A
binding of the target
binding of the outbreak
binding of the antibody
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