| Literature DB >> 8550589 |
R E Hirsch1, M J Lin, G J Vidugiris, S Huang, J M Friedman, R L Nagel, G V Vidugirus.
Abstract
Hemoglobin C (Glu beta 6-->Lys) shares with hemoglobin S (Glu beta 6-->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 Trp beta 15-Ser beta 72 hydrogen bond that most likely leads to a displacement of the A helix away from the E helix.Entities:
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Year: 1996 PMID: 8550589 DOI: 10.1074/jbc.271.1.372
Source DB: PubMed Journal: J Biol Chem ISSN: 0021-9258 Impact factor: 5.157