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Recent structural studies of isolated ACDs from a number of vertebrate sHSPs suggest a variability in the register of the β7/β7 strand interface, which may, in part, give rise to the polydispersity often associated with the full-length proteins.
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Interestingly, the energetic contribution of individual residues to helical or strand interfaces is roughly the same for individual amino acids.
We analyzed the high affinity strand interfaces to assess the relative contribution of individual residues to protein complex formation.
When normalized for natural abundance, we find that nonpolar aromatic residues, histidine, and arginine are overrepresented as hot spots at strand interfaces in comparison to polar residues.
A new design, based on the double-cool-strand interface (DCSI) overcomes these limitations due to: 1) simplicity and low coest, 2) no degradation of labile compounds, 3) no dead volume, 4) optimised chiral MDGC conditions with a single oven, 5) higher sensitivity and peak resolution.
Thus, the strand-strand interface seems to be a favorable crystallographic contact for the PR8 NS1 ED, but may not be physiologically relevant.
The effect of V734Y substitution also suggests that we modeled the β-strand interface in correct position of FilGAP, since in our model this residue at the end of the β-strand.
Our data cannot, however, exclude the possibility that the PR8 ED strand-strand interface is promoted during virus infection by interactions of NS1 with other proteins or by post-translational modifications.
The intra-strand interface makes contacts between adjacent CARDs within the same strand while the inter-strand interface holds the three strands together.
The intra-strand interface is mediated by hydrophobic interactions and hydrogen bonding.
(C ) Effects of mutating the residues at the inter-strand interface and other conserved charged residues on MAVS activity.
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CEO of Professional Science Editing for Scientists @ prosciediting.com