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The model suggests that increasing the size of NCs significantly increases the multivalency but only moderately enhances the binding affinities due to the entropy loss associated with bound receptors on the EC surface.
One of the possibilities to overcome this intrinsic poor acylation efficiency of PBP2a is to design new β-lactams that have improved binding affinities due to increased noncovalent interactions between the inhibitor and the active site.
For example, we found that 36 nt junction probes overlapping a SNP show higher sensitivity towards differential expression, possibly due to alternative splicing brought about by SNPs within splice sites or due to differences in probe binding affinities due to the SNP.
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Our understanding of protein evolution would greatly benefit from mapping of binding landscapes, i.e., changes in protein-protein binding affinity due to all single mutations.
Constructs in which several single domain antibodies are genetically fused serially, as well as those in which single domain antibodies are genetically linked with domains that naturally form multimers, yield improvement in apparent binding affinity due to avidity.
Our data may be an overestimate of the binding affinity due to the difficulty of purifying sufficient soluble WW-domain proteins at a concentration greater than twice the calculated KD.
Moreover, the use of a mutated DAPK catalytic domain relaxed the dimerization capability, allowing us to distinguish a modification of the probe binding affinity due to experimental conditions (seen both with the wild type and the mutated core domain of the kinase) or due to dimerization (only seen with the wild type core domain).
This is significant in the context of TR/pMHC interaction because mutating specific charged interacting residues on pMHC interfaces is known to cause increase or decrease in experimentally determined TR/pMHC binding affinity due to increased or decreased electrostatic interactions between the TR and pMHC leading to an enhanced or reduced T cell response, respectively [29].
They found that the transcriptional activity of ARGHEF10 was affected by differentiated Sp1 binding affinity due to rs4376531.
Saturating amounts of ISCU2 and FXN were used for subsequent activity measurements to remove complications from changes in binding affinity due to the incorporated ISCU2 mutations.
28 It is generally agreed that when resistance to PIs develops there is a decreased binding affinity, due to faster dissociation rate.
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