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The cation-selective diffusion layer, formed with multivalent phosphate or sulfate, contributes hydrogen ions depleted at the interface to form an oxide film leading to the oxide-film-induced passivation (eg, NiNiO).
In the Pikp-HMA/AVR-PikD complex, the AVR-PikDHis46 side chain is buried within a pocket on the Pikp-HMA surface that contributes hydrogen bonds/salt bridge interactions.
Figure 5 shows the positions of cyanide and H2O/OH− relative to the conserved residues that make up the proton transfer network, Lys587, His113, His116, His119, His122, and Asn284, which is probably not directly involved in proton transfer but contributes hydrogen bonds that may be structurally important.
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And although researchers still argue about the precise composition of Earth's early atmosphere, most agree that volcanic eruptions would have contributed hydrogen sulfide, he adds.
Ferric forms insoluble compounds in water, near pH 7. Salt of ferric Fe hydrolyzes water and produces Fe III) oxide-hydroxides thus contributing hydrogen ions to the solution and ultimately pH is decreasing.
The synthetic phenols disrupt free-radical oxidation chain reactions by contributing hydrogen from the phenolic hydroxyl groups thereby forming stable free radicals which do not promote oxidation of lipids.
The monomer-monomer interface of the S. pneumoniae enolase is similar to that of other enolases in the amount of buried surface area; groups contributing hydrogen bonds or electrostatic interactions in the yeast dimer interface [5] are also present in the S. pyogenes and S. pneumoniae enolases.
The majority of the interaction is formed with a monomer of Pikp-HMA, with 87.5% of the effector's buried surface area (902.2 Å) and nine residues contributing hydrogen bond and/or salt bridge interactions.
Vacancy-hydrogen complex contributes to hydrogen embrittlement and induces degradation of mechanical properties [6].
In the CrSPI-1: subtilisin complex, the P1 residue His3 of the CrSPI-domain 1 contributes 5 hydrogen bonding contacts (or 45% of the total hydrogen bonding interactions) with subtilisin.
Fg αPhe564 contributes two hydrogen bonds with BbpAsp334 and Ile335 in the loop region between the C and D strands in N2 domain.
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