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Published online before print July 5, 2006, 10.1110/ps.062272306
Protein Science (2006), 15:1961-1967. Published by Cold Spring Harbor Laboratory Press. Copyright © 2006 The Protein Society
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Circular dichroism spectroscopy of tertiary and quaternary conformations of human hemoglobin entrapped in wet silica gels

Luca Ronda1, Stefano Bruno1, Cristiano Viappiani2, Stefania Abbruzzetti2, Andrea Mozzarelli1, Kenneth C. Lowe3 and Stefano Bettati1

1 Department of Biochemistry and Molecular Biology, University of Parma, 43100 Parma, Italy
2 Department of Physics, University of Parma, 43100 Parma, Italy
3 School of Biology, University of Nottingham, NG7 2RD Nottingham, UK

(RECEIVED April 6, 2006; FINAL REVISION May 15, 2006; ACCEPTED May 16, 2006)

The relative contributions to changes in visible and near UV circular dichroism spectra of hemoglobin of heme ligation and tertiary and quaternary conformational transitions were separated by exploiting the slowing down of structural relaxations for proteins encapsulated in wet, nanoporous silica gels. Spectral signatures, previously assumed to be characteristic of T and R quaternary states, were demonstrated to be specific to different tertiary conformations. The results support the view that ligation and allosteric effectors can modulate the structural and functional properties of hemoglobin by regulating the equilibrium between the same tertiary species within both quaternary states.

Keywords: allosteric effectors; conformational transitions; protein immobilization; heme proteins


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