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When an antigen-antibody interaction takes place the possibility of establishing a second interaction depends on the valence, orientation and flexibility of the antigen-binding site.
The AUCROC for L55-Bound and L55-Unbound are 0.968 and 0.967, respectively, when both structure features (side chain orientation and flexibility) and sequence conservation are used.
Crystal structures of isolated DnaK NBDs in various nucleotide states have failed to capture the delicate intersubdomain allostery that modulates substrate binding affinity, whereas solution-state NMR spectroscopic studies have instead demonstrated that ATP or ADP binding significantly alters NBD subdomain orientation and flexibility.
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However, it is difficult to obtain a solid value of arm size for each fluorophore due to other factors such as orientation, folding and flexibility in molecular arrangement.
EXIA2 is primarily based on the intrinsic structure features, side chain orientation, and structure flexibility, of the input protein.
The results indicate that EXIA2, which uses side chain orientation and structure flexibility, is more effective than the structure features used by POOL.
The performance of EXIA2 is mostly contributed from the intrinsic properties of input structure, the side chain orientation, and structure flexibility feature.
The orientation and rotational interdomain flexibilities of FNIII modules are known to be affected by neighboring domains, so the inclusion or exclusion of alternatively spliced domains may change the global conformation of FN, affecting the presentation of FNIII loop structures and binding sequences to modulate FN-cell signaling and FN-FN interactions during matrix assembly [ 9, 28- 33].
Some of this difference might be explained by conformational flexibility of the noncovalently cross-linked helices in these simulations, the fact that two S H bonds exist in the mutated and reduced transporters (up to ∼1 Å each depending on the orientation), and the need for flexibility in the mutated structures to accommodate the employed oxidant.
Our findings reveal surprising flexibility in orientation and phasing for a nucleosome particle that is tightly confined within an asymmetric ∼80-bp DNA loop.
The SHDW-Yfrac and SHDW-Ylength encode information about size, shape and orientation, and ø expresses the conformational flexibility of a molecule (Dimitriou-Christidis et al., 2008).
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