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All LRR variants are predicted to be destabilizing by at least three methods, meaning that all variants could have a negative structural change (Table S1).
All mutations except one (p.S473L) were predicted to be destabilizing by at least two of the computational methods used (Table S1).
Val160Gly was predicted to be destabilizing, whereas Lys103Met was predicted to be stabilizing.
Thus, all trinucleotide bulges will be predicted to be destabilizing, regardless of bulge and closing pair sequence.
The folding free energy (ΔΔG) of model2 Amber and Charmm were both predicted to be destabilizing; however, the ΔΔG of model3 Amber was predicted to be stabilizing.
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On the other hand, G-quadruplex-forming sequences that favor an all-parallel propeller fold are now predicted to be markedly destabilized if thymine photodimers are formed in their loop regions.
All of the other servers also predicted this mutation to be destabilizing (Supplementary material, Table S1).
Substitution of proline to serine is predicted to be highly stabilizing for residue 145 (ΔΔG = −2.77 kcal mol-1), but highly destabilizing for residue 69 (ΔΔG = 5.23 kcal mol-1).
Because a β-alkyl substitution destabilizes the adjacent bond more than a β-nitrate, the ketones predicted to be formed from breaking the weakest C C bond in α-pinene and Δ-3-carene are structurally very different.
This proposition contrasts with previous theories that predicted populations to be destabilized and communities to be stabilized [4], [8], but is in agreement with other conceptual models [9] [11].
However, such losses are less likely to be destabilizing to the system.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com