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On the other hand, the EcAppA mutants that adopt N-glycosylation motifs from CbAppA showed improved thermostability that three mutants carrying single N-glycosylation motif exhibited 5.6 9.5% residual activity after treatment at 80 °C (1.8% for wild type).
This provides a selective pressure to enrich for mutants that adopt the spore cell fate.
Muller et al. showed that HSP90 is required to fold mutants into the native conformation or, alternatively, forms a stable complex with mutants that adopt an unfolded conformation.
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In contrast, the ability to adopt the shifted conformation of stem-loop I is a major determinant of binding: mutants that cannot adopt this conformation bind much more weakly than wild-type and mutants with a constitutively shifted stem-loop I bind much more strongly.
These predictions, however, are not consistent with the smaller, round nuclei in crwn1 mutants that do not adopt the elongated spindle shapes typical of wild-type nuclei in many cell types.
Because we demonstrated in our initial structure paper that wild-type vcCNT exists as a trimer both in detergent micelles and in the membrane, the similar elution volumes of the mutants strongly suggest that the mutants adopt trimer stoichiometry as well.
Collectively, these data suggest that WT and mutant SOD1 adopt conformations that do not favor co-assembly into higher order structures.
To begin to understand the mechanism of CHD, we adopted the DamID method and identified targets of NKX2-5 muthats that mimic those found in CHD.
We hypothesized that at high temperatures mutants of Cdc10 adopt conformations that are incompatible in association with wild-type Cdc3, but certain substitutions might render Cdc3 capable of "rescuing" the Cdc10 mutants by interacting with them, thereby bypassing the apparent requirement for nucleotide in high-temperature G heterodimerization.
The MD simulations suggested that one of these mutants would adopt the target monomeric structure, which was subsequently confirmed by X-ray crystallography.
Essential subspace overlap analyses were performed to quantitatively distinguish the preference for conformational transitions between states of the gp120 mutants and further to ascertain what kind of conformational state that the mutants prefer to adopt.
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