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These non-binding sites are characterised by sparse opportunities for H-bonding or favourable polar interactions, as reflected by their poor energies of association (Figure 6). Figure 6 shows the relative energy of association for each of the ligand-receptor models.
The three high-affinity Sre1 binding-sites are characterised by a conserved ATC at the 5' end and a conserved AT at the 3' end, while the remaining parts are highly variable (5'-ATCNNNNNAT-3').
The Cu(A -binding site is chA -bindingd by a H1(n)-H2(8)-H3 motif and the Cu(B)-binding site by a H1(3)-H2(n)-H3 motis, where n is a variable number of residues between histidines.
Although it does not conform to the class II or class III binding sites which are characterised by X-Hydrophobic-X-Hydrophobic or X-Neg charged-X-V/I/A, there is variation and other sequences will bind as well.
The dam site is characterised by massive and jointed-phyllites associated with major and minor shears.
Here, these binding sites are not discussed one by one.
These binding sites are highly charged.
Noteworthy, these binding sites are juxtaposed to GATA3-binding sites.
The interaction between α-bungarotoxin and linear synthetic peptides, mimotope of the nicotinic acetylcholine receptor binding site, has been characterised extensively by several methods and a wealth of functional, kinetic and structural data are available.
An HNF4α binding site has been characterised in the PXR promoter that is necessary for expression of PXR in fetal hepatocytes [ 97].
Potential binding sites were elucidated by docking.
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