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We show that the method generates binding surfaces that are more conformationally restricted than previous design methods, reducing opportunities for off-target interactions.
Consequently, the number of protein residues interacting with amino acids/dipeptides is low for the binding surfaces that are highly exposed to solvent.
Secondly, the model shows how buried sequences within the core propeller blades may potentially be exposed by extrusion to provide binding surfaces that are not exposed in the monomeric state.
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Trying to design a binding site in the core of the protein is problematic because it will likely have a negative effect on the stability of the protein, while creating a binding site on the surface of the protein is difficult because there are possibly not enough side chains to contact the ligand from several sides and thus form a binding surface that is complementary in shape to the ligand.
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].
It could be therefore surmised that decorin could antagonize tumor growth by binding to collagen, covering the collagen surfaces that are responsible for the stimulatory effect.
The binding pockets also displayed electrostatic surfaces that were complementary to the hydrophobic nature of COP, SQA, and POR, and the negatively charged HSL.
Upon analyzing the results on isolated proteins and benchmarking against antibody complexes, it is found that the method successfully identifies binding sites located on the protein surface that are accessible to putative binding partners.
In recent work[ 27] we demonstrated that the analysis of Godefroy et al.[ 32] for proton electron dipole coupling is extensible to proton proton dipole coupling, albeit with a much weaker coupling constant.[ 33] In the absence of paramagnetic species, it is the active binding sites on the pore surface that are considered to be the relaxation sinks.
Burgoyne et al. [ 7] analyze clefts on surface, that are likely to be binding sites.
AdpB, a 29 kDa protein, is the first broad-spectrum ECM (extracellular matrix -binding protein localized on the cell surface that was identified and characterized in Prevotella intermatrix -binding
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