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The thermodynamic and structural changes that accompany cooperative protein−DNA binding are key to the recognition, bending, and unwinding of DNA sites during transcription and replication but are still poorly understood.
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A number of these interactions occur within the structurally conserved domains of MTA1, but others are directed through intrinsically disordered regions that become ordered on binding and are key to forming a stable NuRD complex.
These amino acids either are involved in domains within AANATA that overlap between the acetyl-CoA and amino donor binding pockets or are key to maintaining the AANATA structure in a conformation that is optimal for substrate binding.
These latter residues, which are key to binding the benzyl modification of high affinity inhibitors such as BAU, are also the only distinguishing active site residues when comparing eukaryotic and prokaryotic enzymes (equivalent E. coli residues are Ile 220, Val221 and P229).
Identification of the E3 ubiquitin ligase that targets SopB and protein binding partners of ubiquitinated SopB are key to clarifying the contribution of ubiquitination to activity and/or localization of this Salmonella effector.
This observation suggested that the S2 to S4 segments are key to capsaicin binding, while the remaining gating machinery required for capsaicin activation is preserved in both channels.
Strong Hg/Se binding may be key to understanding the biological and environmental behavior of both mercury and selenium (38– 40).
Because Dvl proteins (Dvl1, Dvl2, and Dvl3 in mammals) play diverse roles in Wnt signaling [ 109], identification of their binding partners is key to understanding their biological functions.
A quantitative understanding of interactions between transcription factors (TFs) and their DNA binding sites is key to the rational design of gene regulatory networks.
This suggests additional complexity in TOX3 gene regulation, where a narrow range of FOXA1 binding may be key to appropriate enhancer function.
Since the initiation of transcription is one of the most important steps in gene regulation [ 4], a quantitative understanding of interactions between transcription factors (TFs) and their DNA binding sites is key to predicting the dynamics of gene circuits.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com