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From the FRET measurements alone, we cannot determine potential binding interfaces of the compound to SERCA, but we speculate that these compounds do not bind to the SERCA2a-PLB interface, but rather affect FRET through allosteric changes in SERCA itself.
However, these structures did not define the binding interfaces of the evolutionarily conserved nuclear actin and actin-related proteins (Arps) of INO80 or provide insights into their functional properties10,11,12,13.
Trp is also enriched at protein/protein binding interfaces of the small envelope protein of the hepatitis B virus [55] and of membrane proteins in general [56].
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The autoinhibition model that we propose for BIN1 is shown schematically in Figure 9. BIN1 is in an inhibited state via the interaction between PI 4,5 P2 sensing motif exon10 and SH3 domain, consistent with an earlier study showing that the exon10 peptide binds to the SH3 domain in a region overlapping with the binding interface of the proline-rich domain.
Grizot, S., Duclert, A., Thomas, S., Duchateau, P. & Paques, F. Context dependence between subdomains in the DNA binding interface of the I-CreI homing endonuclease.
The combination of experimentally determined thermodynamic parameters, structure-based calculations, and 15N NMR relaxation analysis highlights the energetic contribution of conformational entropy change upon the complex formation, and water molecules structured in the binding interface of the nSH3 PRM complex.
The binding interface of the FUNDC1 peptideptide on LC3B provides the structural elucidation for the specific recognition.
In summary, we have elucidated the structures of the HBGA binding interface of the GI.8 BV that represents a unique evolutionary path selected by the host HBGAs.
When proteins interact, the binding interface of the interaction is generally localized to specific conserved segments of the interacting proteins that are broadly known as domains.
Residue decomposition of the binding free energies with backbone and side chain contributions as well as their energetic constituents identify the hotspots in the binding interface of the structures.
The binding interface of the GI strains (Norwalk virus) is constituted by three groups of amino acids from the P2 subdomain and positioned mainly in one P monomer, although it is near the interface of two P monomers of the Norwalk virus P dimer.
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