Correlation of protein functional properties in the crystal and in solution: the case study of T-state hemoglobin.
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.
Noble
Robert W
RW
Department of Medicine, State University of New York (SUNY) at Buffalo, Veterans Administration Medical Center, 3495 Bailey Avenue, Buffalo, NY 14215, USA. noble@acsu.buffalo.edu
Kwiatkowski
Laura D
LD
Hui
Hilda L
HL
Bruno
Stefano
S
Bettati
Stefano
S
Mozzarelli
Andrea
A
D000328:Adult; D018360:Crystallography, X-Ray; D006454:Hemoglobins / Q000737:chemistry / Q000502:physiology*; D006801:Humans; D007700:Kinetics; D010100:Oxygen / Q000378:metabolism; D012996:Solutions; D013329:Structure-Activity Relationship
D006454:Hemoglobins; D012996:Solutions; D010100:Oxygen