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Protein Science (2002), 11:1845-1849.
Copyright © 2002 The Protein Society

FOR THE RECORD

Correlation of protein functional properties in the crystal and in solution: The case study of T-state hemoglobin

Robert W. Noble1, Laura D. Kwiatkowski1, Hilda L. Hui1, Stefano Bruno2, Stefano Bettati2,3,4 and Andrea Mozzarelli2,4

1 Department of Medicine, University at Buffalo, Veterans Administration Medical Center, Buffalo, New York 14215, USA
2 Department of Biochemistry and Molecular Biology, University of Parma, 43100 Parma, Italy
3 Department of Public Health, University of Parma, 43100 Parma, Italy
4 Italian National Institute for the Physics of Matter, University of Parma, 43100 Parma, Italy

Reprint requests to: Robert W. Noble, Department of Medicine, University at Buffalo (SUNY), Buffalo VA Medical Center, 3495 Bailey Ave., Buffalo, New York 14215, USA; e-mail: rnoble{at}acsu.buffalo.edu; fax: (716) 862-6526.

The relevance of three-dimensional structures of proteins, determined by X-ray crystallography, is an important issue that is becoming even more critical in light of the Structural Genomics Initiative. As a case study, a detailed comparison of functional properties of the T quaternary states of genetically or chemically modified human hemoglobins (Hbs) in solution and in the crystal was performed. Oxygen affinities of Hbs in crystals correlate with the rate constants of their initial combination with carbon monoxide (CO) in solution, indicating that changes in ligand affinity caused by the modifications are similarly observed in both physical states.

Keywords: Hemoglobin; T quaternary structure; ligand affinity; mutational effects; properties in solution; properties in crystals

Abbreviations: PEG, polyethylene glycol • IHP, inositol hexaphosphate • HbA, human adult hemoglobin • Hb, hemoglobin • desArg, human hemoglobin from which the C-terminal arginines of the {alpha} subunits have been enzymatically removed • desHis, human hemoglobin from which the C-terminal histidines of the ß subunits have been removed • deoxyHb, deoxygenated or unliganded hemoglobin


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