Gary Ackers Professor - Emeritus Dept. of Biochemistry and Molecular Biophysics

Research Interests

Physical basis of biological control; protein-nucleic acid interacting systems

Selected Publications

• Holt, J.M. and Ackers, G.K. The Hill coefficient: Inadequate resolution of cooperativity in human hemoglobin. Methods Enzymol 455:193-212 (2009).

• Ackers, G.K. and Holt, J.M. Asymmetric cooperativity in a symmetric tetramer: Human hemoglobin. J Biol Chem 281:11441-11443 (2006).

• Aquerra, R.M., Kliger, D.S., Holt, J.M. and Ackers, G.K. The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 2. Cooperative free energies of (aFeCOßFe)2 and (aFeßFeCO)2 T-state tetramers. Biochemistry 43:12065-12080 (2004).

• Goldbeck, R.A., Esquerra, R.M., Holt, J.M., Ackers, G.K. and Kliger, D.S. The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 1. Microstate linear free energy relations. Biochemistry 43:12048-1204 (2004).

• Ackers, G.K., Holt, J.M., Burgie, E.S. and Yarian, C.S. Analyzing intermediate state cooperativity in hemoglobin. Methods in Enzymology 379:3-28 (2004).