Sentence examples for mutant in complex from inspiring English sources

We also determined the crystal structures of wild-type and the F179I mutant in complex with GalNAc at site II.

The study of tertiary and quaternary structure of PFN1 protein (wild type and mutant) in complex with actin and/or PLP requires an extensive set of molecular dynamics simulations.

A structure determination of the mutant in complex with an ATP-analogue confirmed the predicted change of the purine base binding plane orientation.

Br-HIBO displays selectivity among different AMPA receptor subunits, and the design and structure determination of the S1S2J-Y702F mutant in complex with Br-HIBO and ACPA have allowed us to explain the molecular mechanism behind this selectivity and to identify key residues for ligand recognition.

The structures of an E541A mutant in complex with a natural β-1,4-d-glucosamine tetrasaccharide substrate and both E541A and D469A mutants in complex with a pNP-β-d-glucosaminide synthetic substrate provide insight into interactions in the + 1 subsite of this enzyme.

The crystallographic asymmetric unit of the PDE9Q453E mutant in complex with IBMX or (S -BAY73-6691 containS -BAY73-6691es of the PDE9A2 containsc domain.

For example, Leu111 in eNOS is in position to possibly clash with the out-rotamer conformation of Tyr477, but the eNOS L111A mutant in complexes with (3 R,4 R) - 3 or (3 R,4 R) - 5 shows that Tyr477 remains in place and does not adopt the out-rotamer conformation.

e, Analytical SEC of TfR1 mutants in complex with Tf. f, Circular dichroism spectra of recombinant TfR1 mutants.

Furthermore, we obtained the X-ray structures of the PI3Kα mutants in complex with the ATR inhibitors.

In addition to the wild-type, this study also looks at specific XPA67-80 mutants in complex with the ERCC1 central domain and thus contributes to defining the conformational determinants for binding, as well as all of the essential structural elements necessary for the rational design of an XPA-based, ERCC1-specific inhibitor.

A comparison of the average B-factors of the C3 methyl acetate group in the three structures shows averages of 21.2, 13.9, and 27.9 Å for the single, double, and triple mutants in complex with cefotaxime, respectively.