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The overall structures of MHETase and FaeB are structurally similar (2.04 Å RMSD for 421 out of 559 residues aligned) despite a relatively low number of amino acid identities (27.5%).
Structural alignment with aSelB [ 27] shows that the overall structures are remarkably similar.
Structural comparison indicates that despite slight local secondary structure changes, the overall structures are highly similar (Fig. 1C).
The overall structures are very similar.
Though the two systems differ in several technical respects, they would have similar overall structures.
The two proteins have similar domain arrangements and overall structures with an RMSD of 1.99 Å (Fig. 4e 24.
The design with composite materials could avoid these problems and provide lightness to the overall structures.
The overall structures, especially the residues in some positions of HR2 are highly conserved.
These key residues are not conserved (Supplementary Fig. 4), although generally the JMJ13 and JMJ14 show similar overall structures (Fig. 4e).
(a) Overall structures of the ETB receptor bound to K-8794 (left; turquoise) and bosentan (right; orange), viewed parallel to the membrane plane.
The overall structures show good agreement with both monomers of atypical homodimeric VAP1.
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Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com