| Autor: |
Noble, Robert W., Kwiatkowski, Laura D., Hui, Hilda L., Bruno, Stefano, Bettati, Stefano, Mozzarelli, Andrea |
| Zdroj: |
Protein Science: A Publication of the Protein Society; 2002, Vol. 11 Issue 7, p1845-1849, 5p |
| Abstrakt: |
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. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
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