Conformational changes in oxyhemoglobin C (Gluβ6 → Lys) detected by spectroscopic probing

Rhoda Elison Hirsch, Margaret J. Lin, Gediminas V.A. Vidugirus, Shuocai Huang, Joel M. Friedman, Ronald L. Nagel

Research output: Contribution to journalArticlepeer-review

25 Scopus citations


Hemoglobin C (Glu β6 → Lys) shares with hemoglobin S (Gluβ6 → Val) the site of mutation, but with different consequences: deoxyHbS forms polymers, whereas oxyHbC readily forms crystals. The molecular mechanism for this property of oxyHbC is unknown. Since no detailed oxyHbC crystal structural information exists, spectroscopic probing is used in this study to investigate possible solution-phase conformational changes in HbC compared with HbA. Intrinsic fluorescence combined with UV resonance Raman data demonstrate a weakening of the Trpβ15-Serβ72 hydrogen bond that most likely leads to a displacement of the A helix away from the E helix.

Original languageEnglish (US)
Pages (from-to)372-375
Number of pages4
JournalJournal of Biological Chemistry
Issue number1
StatePublished - Jan 5 1996

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology


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