Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange.

@article{Plesniak1996CharacterizationOA,
  title={Characterization of a buried neutral histidine residue in Bacillus circulans xylanase: NMR assignments, pH titration, and hydrogen exchange.},
  author={Leigh A. Plesniak and Gregory P Connelly and Warren W. Wakarchuk and Lawrence P. McIntosh},
  journal={Protein science : a publication of the Protein Society},
  year={1996},
  volume={5 11},
  pages={2319-28}
}
Bacillus circulans xylanase contains two histidines, one of which (His 156) is solvent exposed, whereas the other (His 149) is buried within its hydrophobic core. His 149 is involved in a network of hydrogen bonds with an internal water and Ser 130, as well as a potential weak aromatic-aromatic interaction with Tyr 105. These three residues, and their network of interactions with the bound water, are conserved in four homologous xylanases. To probe the structural role played by His 149, NMR… CONTINUE READING
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