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A further residue that when mutated gave a strong effect on planar polarity but not on canonical activity (E279) protrudes into the deep central pocket in our model and thus might be part of a specific binding surface that interacts directly with Dsh only when the Fz receptor adopts a certain conformation.
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Each motif is predicted to comprise two anti-parallel α-helices that contain several projecting amino acidic side groups; therefore the arrays would form a superhelix with a binding surface that is suitable to interact with selected bases [ 19] and phosphate groups of RNA molecules [ 20].
This cluster comprises a large hydrophobic surface that interacts directly with IL-1α, as discussed below.
Each of Glo's RNA-binding domains therefore contains two distinct binding surfaces that interact with different types of RNA target sequence.
Consequently, the number of protein residues interacting with amino acids/dipeptides is low for the binding surfaces that are highly exposed to solvent.
The projection of the P+3 substrate residue inward toward a pocket formed by the rearranged C-loop may provide a binding surface for small molecules that interact with a particular substrate sequence at this position.
Since both RNA binding surfaces of Hfq interact with the fhlA leader, multiple footprints were expected.
S100B is a calcium-sensor protein, and upon Ca2+ binding it exposes hydrophobic surfaces that interact with target proteins [17]-[20] [17]-[20]
However, it shows similarities in the oligonucleotide binding surface to canonical RRMs and interacts with yeast total RNA.
Furthermore, we demonstrate via surface plasmon resonance (SPR) binding assays that 13m interacts robustly with recombinant HIV-1 CA and exhibits antiviral activity in both the early and late stages of HIV-1 replication.
Pathogenic Gram-negative bacteria have developed many distinct secretion mechanisms for the efficient surface display of binding domains that specifically interact with their complementary receptors on host cell surfaces [1], [2].
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CEO of Professional Science Editing for Scientists @ prosciediting.com