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The binary complex containing the RecA2 domain of Mss116 bound to an RNA duplex (PDB code: 4DB2) is colored cyan and aligned to the ternary complex.
Note that the 1D H NMR spectrum of the binary complex containing the 3′SL RNA reflects only the unbound nucleic acid that is in equilibrium with the enzyme.
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Furthermore, binary complexes containing the entire functional core of PPP1R15B require the presence of actin for stability and solubility.
Δlog10 β was not calculated for histidine because the stability constant of the binary complex containing two protonated amino acids (Table 1) is unavailable.
Previously, the X-ray structure of the similar binary complex containing phosphorylated SP20 has been reported.
In addition to alterations in the fingers, the DNA bound to the I707L mutant also adopts a dramatically different structure than two different wild-type binary complexes containing an 5′-AAAG overhang (4KTQ.pdb and 3SZ2.pdb).
Mutation of this residue suggests that the role of Lys differs when the repair reaction can be handled by a single polymerase (gapped substrate) or when a synapsis is required (two binary complexes containing 3′ overhangs).
In contrast to Kf-exo–, the binding in the binary complex between the modified template and pol β is less tight than that in the complex containing the unmodified template, where the differences in binding are approximately 3-fold for FABP and 5- to 6-fold for FAAF, respectively.
For example, HlMyb3 variants and all complexes containing the HlMyb3 gene peaked at 4 days post infiltration (dpi), whereas the HlMyb2 gene reached maximum activity 66-68 h dpi, except for the M2W1 binary complex.
During the entire polymerization reaction, the inorganic diphosphate product will release from the ternary complex, thus yielding another defined binary complex that contains the bound polymer substrate ready for the subsequent second half-reaction (next nucleotide incorporation).
The three complexes contain the {GaIII2 μ-OH 2}4+ core.
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