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The photounbinding performance of four CaM binding peptides with different binding affinities to calmodulin - spanning three orders of magnitude - were compared at various laser intensities.
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We present studies of the photounbinding of labeled calmodulin (CaM) from a set of CaM-binding peptides with different affinities to CaM after one- and two-photon excitation.
To represent diverse binding modes, 9 peptides with different sequences and structures were used.
We observed that some PDZ domains share identical subsequences in the 10 and 16 binding positions but bind the same peptides with different affinity.
This dimorphism appears to be associated with the selection of binding-peptide groups with different motifs (Verreck et al. 1996).
Thus, a variety of different peptides with different binding properties, in the low nanomolar and subnanomolar range, have been developed [ 97].
Moreover, 28 (39%) of the patients had antibodies with overlapping specificities, so that the binding could be inhibited by peptides with different ureido group-containing amino acids.
We evaluated several conditions for phage targeting of the grafting material including 1) different starting peptide libraries, 2) different elution strategies, 3) different blocking strategies and 3) different formulations of the matrix material to facilitate selection of peptides with different binding characteristics.
Two RGD peptides with different integrin-binding specificities were added to the polyethylene glycol hydrogels.
Three new 1,4,7,10-tetraazacyclododecane-1,4,7,10-tetraacetic acid (DOTA -linker-d-Phe- d-Lys6-GnRH) peptiDOTA -linker-d-Phe- d-Lys6-GnRHlinkers were DOTA -linker-d-Phe- d-Lys6-GnRHcts on GnRH receptor binDOTA -linker-d-Phe- d-Lys6-GnRH
A series of cyclic peptides with different linkers were designed and synthesized to model the elbow-type Ca2+-binding loop of α-lactalbumin (LA).
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