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The designed peptide perfectly covers the binding surface, while the known peptide is more distant to the surface.
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In the "cis" model the N-terminal DID-DD region directly occludes the actin binding surface of the FH2 dimer while in the "trans" model the DID-DD region is maintained at a distance from the surface of the FH2 domain by the long αT helix, which extends from the FH2 domain to present the DAD segment for binding.
These results suggest that the Met4-Cbf1 binding surface is distinct from the Met4-Met31 surfand, and that the Met4-TFIID binding surface is closer to the Met4-Met31 surface, placing the Met4-TFIID binding surface near the 3' edge of the complex.
This binding surface overlaps the site for RbBP5.
Its binding surface on the protein is carpeted by an electropositive surface potential.
HOTTIP lncRNA binding surface overlaps with the RbBP5 binding surface on WDR5.
One can observe that the drug binding surfaces are closed off from the extracellular space in the fully opened inward conformation, while access to the extracellular space increases with each step toward the fully opened outward conformation until a large portion of the drug binding surface is exposed to the outside of the cell in the fully opened outward conformation.
For type II AFPs, two disulfide bonds are critical to stabilize the ice-binding surface in the solution, while the sugar-binding activity may require the binding site to be more flexible, hence disfavoring the presence of multiple disulfide bonds.
Additionally, SiteMap identified two binding locations under the third condition (at either end of the peptide), while the center of the peptide was excluded from the binding surface.
This suggests that the binding of MB onto TISW would be least favourable by heterogeneous surface, while the binding of Cd2+ onto TISW would be most favourable by heterogeneous surface (({{0 < 1} mathord{left/ {vphantom {{0 < 1} n}} right. kern-0pt} n} < 1 -favourable, ({1 -favourablet/ {1phantomathord{left/t. kern-0pt} n} > 1)-non favourable).
(A ) The binding surface for Pins in GKPIDs is derived from the GMP-binding surface of gk enzymes.
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