Quaternary structure sensitive tyrosine interactions in hemoglobin: a UV resonance Raman study of the double mutant rHb (beta99Asp-->Asn, alpha42Tyr-->Asp).

@article{Huang1997QuaternarySS,
  title={Quaternary structure sensitive tyrosine interactions in hemoglobin: a UV resonance Raman study of the double mutant rHb (beta99Asp-->Asn, alpha42Tyr-->Asp).},
  author={Shuyan Huang and Eric Scott Peterson and C Ho and Jonathan M. Friedman},
  journal={Biochemistry},
  year={1997},
  volume={36 20},
  pages={
          6197-206
        }
}
Two interactions involving tyrosines have been implicated in the communication pathway that links ligand binding to quaternary state changes in hemoglobin. Tyr alpha(1)42 stabilizes the alpha1beta2 T state interface through the formation of a hydrogen bond to Asp beta(2)99. The side chains of the penultimate Tyr residues (alpha140 and beta145) occupy the pockets made by helicies F and H in the deoxy form with the phenolic hydroxyl hydrogen bonded to the carbonyl group of Val FG5. Early… CONTINUE READING

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