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Ligand binding produces conformational changes in receptors that alters the alignment of receptor-associated JAKs, enabling phosphorylation of specific tyrosine residues that converts inactive JAKs into a catalytically active tyrosine kinases (Brooks et al, 2014).
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Upon an increase in intracellular free calcium level the binding of Ca2+ to TnC produces conformational changes to other proteins of the troponin complex.
2. At low water activity, the reduced hydration produces conformational changes in the enzyme, affecting its catalytic activity.
These mutations produce conformational changes that reveal novel antibody binding epitopes.
Zinc binding to the WCBD has also been characterized by circular dichroism spectroscopy and shown to produce conformational changes that are completely different from those induced by copper.
GTP binding produces a conformational change in Rho leading to interaction with and activation of downstream effector proteins, such as Rho kinase (ROCK) for RhoA and RhoC, or p21 activated kinase (Pak) for Rac and Cdc42 [ 16- 18].
One element of the allosteric mechanism that produces the conformational changes through propagation of local perturbations, rather than large rigid body motions, is the effect of ligand binding in the extracellular vestibule of LeuT, termed the S2 binding site [29].
CFTR is apparently unique in the ABC transporter family of proteins in that binding and hydrolysis of ATP, catalyzed by the cytoplasmic nucleotide binding domains, produce a conformational change that opens an anion conduction path through which chloride can move by electrodiffusion (1− 4).
The ATPase activity of T. maritima CopA is dependent on copper within the micromolar range (40), suggesting that copper binding may produce a conformational change involved in catalytic activation.
Thus, binding to ATP or ADP produces a conformational change that enables the N-terminal domain to become accessible for client protein binding.
Calcium binding to an S100 protein produces a conformational change that exposes a hydrophobic surface, allowing recruitment of other proteins that leads to a biological response.
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