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To overcome these drawbacks, previous studies have used heparin for the controlled and sustained release of BMP-2 because heparin is well known to have not only good binding affinities for various growth factors but also the ability to regulate the release of growth factors [ 27– 35, 35– 35].
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Because MHC alleles differ in their binding affinity for various peptides, a vaccine based on just one peptide may not work for everyone.
However, isoform-specific differences exist in terms of binding affinity for various ligands [ 3].
This means that its binding affinity for various antigens (epitopes) varies depending on the specific inter-atomic interactions occurring between its idiotope and the antigen epitope.
To better understand the possible role of Srs2 during PRR and HR, we examined its binding affinity for various DNA structures that may imitate those found during DNA metabolic processes.
The most abundant and crossreactive of these antibodies (CK3) recognized the biotinylation sequence located at the C-terminus of each chemokine, thus explaining its exquisite promiscuity and similar binding affinities for the various chemokines.
To understand the mechanism of histone H3/H4 transfer among Asf1, CAF-1, and DNA from a thermodynamic perspective, we measured the binding affinities for their various complexes.
The designed peptide demonstrated remarkable cofactor selectivity with a significantly weaker binding affinity for the natural heme cofactor.
When between trial variations in HSP72 binding capacity were observed, relative differences in HSP72 binding affinity for the various peptides were maintained.
If the structural properties of the receptor site are known (for example, there is crystallographic data) then techniques involving approximations of potential functions can be applied to estimate or at least compare binding affinities of various ligands [1].
Next, we measured the binding affinities for BiP's ATPase domain interacting with human Ire1 and Perk luminal domains comprising of various regions between I and V.
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