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The potential finding of a brain-specific nef structure indicates that HAD may result from genetic alterations that alter the folding or binding potential of the protein.
The mutations of key residues significantly alter the folding by distorting the cooperative interactions, which can result in the misfolding or aggregation; nonetheless, the rational design by mutations can be beneficial to protein folding.
Here, we use variants of R16 and R17 to demonstrate that substitution of just five key residues is sufficient to alter the folding mechanism and reduce the landscape roughness.
This mutation may alter the folding of ENT1, thereby reducing the uptake and binding activity of the transporter.
To verify whether the introduced deletion could significantly alter the folding of the DDX3ΔINS mutant, thermal inactivation experiments were carried out.
Likewise the substitution of GFP with another tag that exists as a higher order oligomer could alter the folding of a pathogenic protein to which it is fused, and potentially its lethality.
Similar(33)
NMR and far-UV CD experiments confirmed that the mutations do not affect Josephin secondary and tertiary structure or significantly alter the fold stability (data not shown).
However, L43S/Y45S in VAMP7 longin domain and the three mutations in Hrb were soluble and did not alter the fold of the proteins, as estimated by circular dichroism (data not shown).
Nevertheless, it is possible that CHIP with its co-chaperone function might reduce luciferase activity by directly altering the folding or stability of luciferase independent of α-syn.
We subsequently stored the RNA at −20°C in absence or in presence of 1 mM MgCl2, at pH 5.0, which did not promote RNA degradation (Figure S6) nor altered the folding.
As it was unlikely that the peptide could adopt a PKA-interacting conformation in both the lit and dark state structures, this data suggested that peptide incorporation at this site altered the folding of LOV2.
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