Sentence examples for binary complex with the from inspiring English sources

The 330-nt IRES RNA forms a binary complex with the small 40S ribosomal subunit as a first step in translation initiation.

The structure of the apo-form of this enzyme from Zymomonas mobilis has been solved and refined to 1.9-Å resolution, and that of a binary complex with the co-substrate NADPH to 2.7-Å resolution.

At physiological magnesium ion concentrations, the HCV IRES forms a binary complex with the 40S ribosomal subunit, recruits initiation factor eIF3 and the ternary eIF2/GTP/Met-tRNA(i Met complex, and joins 60S subunits to assemble translation-competent 80S ribosomes.

We have previously designed a variant of tissue inhibitor of metalloproteinase (TIMP -1 bearing a TIMP -1mutation (V4A + P6V + T98L, or N-TIMP-1mt1) that forms tight bearingcomplex with the soluble catriplec domutationMT1-MMP [M.H. Lee, M. Rapti, G. Murphy, J. Biol. Chem. 278 (2003) 40224–40230].

The structure of mouse class II alcohol dehydrogenase (ADH2) has been determined in a binary complex with the coenzyme NADH and in a ternary complex with both NADH and the inhibitor N-cyclohexylformamide to 2.2 Å and 2.1 Å resolution, respectively.

This separation does not occur unless the mismatched P/T is in a binary complex with the pol.

We report here our systematic characterization of the water dynamics at several specific sites of polymerase β in its apo form, the binary complex with DNA, and the ternary state with DNA and an incoming nucleotide.

The linker domain, therefore, visits several potential energy minima in the binary complex with comparable stability during the simulation, while its motion is more confined in the ternary complex trajectory.

In addition, the structure of the apo-PKAc binary complex with SP20 suggests that the sequence of binding events may become ordered in a metal-free environment, with SP20 binding first to prime the enzyme for subsequent ATP binding.

In the structure of the pol λ binary complex with a two-nucleotide gap DNA, the 8 kDa domain binds the 5′-end of the gap, as in the complex with the one-nucleotide gap.

The interdomain FRET changes observed upon mixing a preformed Dpo4·DNA binary complex with dNTP are consistent with the previously proposed nucleotide incorporation mechanism involving pre- and postcatalytic conformational change steps (steps 4 10, Figure 6C).