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All the mutations encode amino acid residues in or around the pore region of the Nav1.8 protein, replacing neutral residues with acidic ones that are attracted to water.
Moreover, residues with significant exchange broadening are found.
However, these chains could be freed by extracting the Fe residues with hydrochloric acid.
(B) Positions of residues with RMSD value larger than 2 Å in the dimeric structures.
Kluyveromyces produced maximum xylitol from acid treated wheat straw residues with enzymatic saccharification.
Extract the residues with 5 mL KH2PO4 solution for another time, merge the two supernatant.
The Cα atoms of residues with large chemical shift changes are shown as pink spheres.
The connection of standard residues with peptidic bonds is again handled with recourse to predefined templates.
(This avoids having to cut the residues with more valuable gas oil to reduce viscosity).
Only the assignments of residues with missing NH signals in holo protein are labeled.
(C) Positions of residues with RMSD value larger than 2 Å in the subunit structures.
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