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Correlation of protein functional properties in the crystal and in solution: The case study of T‐state hemoglobin
Author(s) -
Noble Robert W.,
Kwiatkowski Laura D.,
Hui Hilda L.,
Bruno Stefano,
Bettati Stefano,
Mozzarelli Andrea
Publication year - 2002
Publication title -
protein science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.353
H-Index - 175
eISSN - 1469-896X
pISSN - 0961-8368
DOI - 10.1110/ps.0205702
Subject(s) - hemoglobin , carbon monoxide , affinities , ligand (biochemistry) , chemistry , structural genomics , crystallography , hemeprotein , crystal (programming language) , crystal structure , protein structure , stereochemistry , heme , biochemistry , catalysis , receptor , enzyme , computer science , programming language
Abstract 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.