Sentence examples for binding residues found in from inspiring English sources

Supplementary Figure 6 shows that HAdV-D26/48K HAdV-D26/48K the sialic acidobinotng reshares found in HAdV-G52K or CAV-2 butheo sialicthe Tyr-142 acidLys-178 contact residues with HAdV-D37K.

This is in agreement with the high degree of conservation of the alpha amino acid binding residues found in many amino acid binding VFTs.

Ca2+ was not inhibitory and was agreement with the pullulanase primary structure of PulN lacks typical Ca2+ binding residues found in other members of glycoside hydrolase family 13 [ 12].

The VP1-derived VLPs from two other members of the genus Wukipolyomavirus (KIPyV and WUPyV) differed in their ability to hemagglutinate guinea pig erythrocytes, despite the fact that none of the sialic acid binding residues found in SV40, JCPyV, or MPyV are conserved in the WUPyV and KIPyV VP1 structures [ 73].

CDD searches [45] reveal that SerC1 and SerC2 in K. foliaceum have retained almost all the catalytic, DNA-binding, presynaptic, and synaptic residues found in other site-specific serine recombinases (Figure S3).

HxkC and HxkD are similar in sequence to catalytic hexokinases but lack some of the conserved residues found in the sugar-binding and ATP-binding domains.

By mutating the large residues found in the PFTase binding pocket, we reasoned that it should be possible to accommodate these larger analogues.

Again, the most common residues found in the substrate-binding site are E, and also D. These residues are D130 in the yeast phosphate carrier (Phelps and Wohlrab 1991), E600 in the yeast aspartate/glutamate carrier (Cavero et al. 2003), E91 in the yeast oxodicarboxylate carrier (Palmieri et al. 2000) and E24 in the yeast GTP/GDP carrier (Vozza et al. 2004).

Drug residues found in beef and poultry continue to decline.

The K49E mutation replaces a crucial Lys residue found in the amphipathic binding groove of all 14-3-3 14-3-3 14-3-3lu, thus, abolisoformsost, if not all, interactions of 14-3-3 with its byndinGluarthuss [41].

Trp 470 of PSD95 corresponds to the highly conserved tryptophan residue found in the hydrophobic binding surface of prototypical SH3 domains that mediates interaction with proline-containing peptides (Erpel et al, 1995).