Sentence examples for binding cleft that can from inspiring English sources

There is a Glu166 located at substrate binding cleft that can interact with P3 residue.

Type B CBMs have an open cleft that can bind polysaccharides found in amorphous regions of cellulose and hemicellulose [ 43– 43].

The 6-methyl of the pyrimidine moiety inserts into a pocket at the bottom of the binding cleft that is formed by Tyr34, Met310, Ala205 and Gln230.

The primary binding site is composed of pyrimidine-specific binding clefts that are located in the N-terminal domains and anchor Rho to transcripts at C-rich Rut (Rho utilization) sites.

Large changes in chemical shift were observed in two main regions: the peptide-binding cleft that directly binds the p53 ligands; and the hinge regions connecting the β-sheet and α-helical structures that form the binding cleft.

Children with Pierre Robin syndrome are born with facial deformities like abnormally small lower jaws and cleft palates that can hinder eating and breathing.

Furthermore, the binding cleft can be subdivided into three α-subdomains that consists of two alpha helical regions (α1 and α2) and a third region (α3) that helps in stabilizing the HLA-protein to the cell surface (in addition to the stabilization from β2-m) [7].

Many synthetic models are relatively ineffective given that they have no such binding cleft, although this can be improved somewhat in apolar solvents (and under micellar conditions), which can simulate the apolarity of an active site cleft.

Multimeric proteins composed of identical subunits often form clefts between contact faces that can be mistaken as binding sites (Figure 11). Figure 11 Pocket prediction for influenza virus neuramidase (PDB: 1a4g).

The binding of the PEG molecule traces out the better part of the substrate-binding cleft showing that HoBGLA can indeed accommodate extended molecules, which is relevant for synthesis of longer GOS products.

Interactions between trimers in these larger oligomers are further facilitated because substrate binding also induces the displacement of a polar surface in the PDZ1 domain that leads to the exposure of a hydrophobic cleft in this domain that can now interact with a matching hydrophobic patch in the surface of the PDZ2 domains of an adjacent trimer.