CONFORMATIONAL-CHANGES IN OXYHEMOGLOBIN-C (GLU(BETA-6)-]LYS) DETECTEDBY SPECTROSCOPIC PROBING

Authors
HIRSCH RE LIN MJ VIDUGIRUS GVA HUANG SC FRIEDMAN JM NAGEL RL
Citation
Re. Hirsch et al., CONFORMATIONAL-CHANGES IN OXYHEMOGLOBIN-C (GLU(BETA-6)-]LYS) DETECTEDBY SPECTROSCOPIC PROBING, The Journal of biological chemistry, 271(1), 1996, pp. 372-375
Citations number
24
Categorie Soggetti
Biology
Journal title
The Journal of biological chemistry → ACNP
ISSN journal
00219258
Volume
271
Issue
1
Year of publication
1996
Pages
372 - 375
Database
ISI
SICI code
0021-9258(1996)271:1<372:CIO(D>2.0.ZU;2-1
Abstract
Hemoglobin C (Glu(beta 6) --> Lys) shares with hemoglobin S (Glu(beta 6) --> Val) the site of mutation, but with different consequences: deo xyHbS forms polymers, whereas oxyHbC readily forms crystals. The molec ular mechanism for this property of oxyHbC is unknown, Since no detail ed oxyHbC crystal structural information exists, spectroscopic probing is used in this study to investigate possible solution-phase conforma tional changes in HbC compared with HbA. Intrinsic fluorescence combin ed with UV resonance Raman data demonstrate a weakening of the Trp(bet a 15)-Ser(beta 72) hydrogen bond that most likely leads to a displacem ent of the A helix away from the E helix.