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This seems to be a reasonable result because, even more than 500 million years after the divergence between humans and squids, DNA binding proteins are usually included among highly conserved genes due to selection pressure [ 24- 27].
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Disordered proteins are usually involved in folding upon binding [ 28].
Intrinsic metal binding to proteins is usually entropically driven (ΔH>0) due to the very high dehydration energies of divalent cations.
The PLG binding to receptor proteins is usually mediated by a carboxyl-terminal lysine residue.
During ChIP-seq, DNA binding proteins are treated with a fixative agent, usually formaldehyde, and cross-linked to their bound DNA before it is extracted and the chromatin sheared to a size of 100-300 bp [ 12, 13].
We can hypothesize that the motifs represents the binding sites for some proteins responsible for these changes in expression, but the identity of the proteins is usually unknown.
We show that dsRNA-binding proteins are prominent autoantigens.
No Vn-binding proteins were detected in the weak Vn-binding strain KR497 (data not shown).
Similarly, sugar-binding proteins in yeast are usually denoted by their functions in flocculation and in adhesion.
As a Ca2+-binding protein, PVAL is usually present in high concentrations in fast muscle cells, to a lower extend in specific neurons of the central and peripheral nervous system, and in cells of endocrine glands [ 53].
Mutated amino acids are normally involved in drug binding and are usually restricted within a short stretch of the protein termed the rifampicin resistance determining region (RRDR) [ 19].
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