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Receptor adherence in receptor molecular biology is evaluated by receptor affinity, which relates to the strength of interaction between a single antigen-binding site and a single antigenic determinant, as well as by receptor avidity, which represents the strength of binding of a molecule with multiple binding sites, such as the binding of a complex antigen with multiple antibodies.
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Further, analysis by EMSA of the binding of ISGF3 (a complex of STAT1, STAT2 and IRF9) to a DNA probe containing the ISRE of the ISG15 promoter indicated that IFN-α-induced binding to the probe was equivalent within extracts of EBV-negative (A.2) and EBV-positive (A.15) Akata cells for at least 4 h following addition of IFN-α.
RA, a physiologically active form of vitamin A, regulates gene expression by binding to a complex of retinoic acid receptors (RARs) and retinoid X receptors (RXRs).
In eukaryotes this structure involves DNA binding to a complex of small basic proteins called histones, while in prokaryotes multiple types of proteins are involved.
The binding of A to Y results in the complex AY.
Using computational docking, it was possible to identify a shallow carbohydrate-binding site on the IL8 surface and construct 3D models of the binding mode of a complex and highly charged oligosaccharide.
In all cases, increasing the binding affinity of a complex increases its concentration globally, as expected.
In order to detect the interacting transcription factor binding sites of a complex, we examined the positional relationships of words.
It is generally believed that not all amino acids in a protein interface contribute to the affinity of binding of a protein complex in a uniform way, and major contributions to the binding energies of a protein complex are composed from a small fraction of amino acids present in the protein surface, known as hot spots.
The lectin pathway of complement system is initiated by binding of a protein complex consisting of mannose-binding lectin (MBL) and serine proteases, mannose-binding lectin associated proteases 1 and 2 (MASP-1 and -2) to mannans on bacterial cell surfaces, and thus its activation is independent of antibody like alternative pathway.
The repression of gurken translation is thought to be brought about by the binding of a protein complex consisting of Cup, Squid, PABP55B and Bruno to Bruno Response Elements (BREs) located in the 3'UTR of gurken mRNA [26].
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