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The denaturation of many proteins, such as egg white, is irreversible.
Typically, the pH optimum correlates with pH stability, although in many proteins such correlation was not observed, because pH optimum is most important for the adaptation of enzymes to the biophysical characteristics of the corresponding environment (Talley and Alexov 2010).
The cell cycle is driven by ordered and finely regulated proteasomal degradation of many proteins such as cyclins, cyclin-dependent kinase (CDK) inhibitors, and licensing and check point factors.
Integrin downstream signaling involves many proteins, such as FAK, paxillin, α-actinin, vinculin, and many others, that affect actin organization, among other processes [33], [34].
In addition, we identified many proteins such as Apolipoprotein E (gene name Apoe) [40], Peptidyl-prolyl cis/trans isomerase NIMA-interacting 1 (gene name Pin1) [41], and numerous other proteins that have already been implicated in AD.
They interact with features of non-native protein folds that are common to many proteins, such as hydrophobic stretches and unstructured backbone regions, and provide nano-compartments to shield proteins during their folding process from other proteins.
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At the same time, high Pi concentrations may inhibit plant growth because the genes encoding many nuclear proteins, such as poly(A) polymerase (e.g., Os06t0558700), many protein synthesis-related proteins, such as translation initiation factor 2 (e.g., Os03t0296400) and aminoacyl-tRNA synthetases (e.g., Os06t0645400) were downregulated in shoot.
Many proteins mediating such dynamic activities are likely regulated by palmitoylation based on evolutionary conservation [ 1] or results from palmitoyl proteomics [ 5].
Many secreted proteins such as antibodies, growth factors, extracellular matrix proteins, and cell surface receptors or transporters, which happen to be of great therapeutic interest, are rich in disulfide bonds.
Incorporation of inter- or intramolecular covalent cross-links into food proteins with microbial transglutaminase (MTG) improves the physical and textural properties of many food proteins, such as tofu, boiled fish paste, and sausage.
These processes include many regulatory proteins such as SNAREs, Rabs and coats.
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