Gary Keith Ackers
Affiliations: | Washington University, Saint Louis, St. Louis, MO |
Area:
Biochemistry, General BiophysicsWebsite:
http://www.biophysics.org/Publications/Newsletter/PastIssues/August2011/ObituaryGaryKAckers/tabid/2936/Default.aspxGoogle:
"Gary Keith Ackers"Bio:
(1939 - 2011)
https://source.wustl.edu/2011/06/ackers-biophysicist-and-human-hemoglobin-expert-dies-at-71/
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Parents
Sign in to add mentor| Thomas E. Thompson | grad student | 1964 | Johns Hopkins (Chemistry Tree) | |
| (The molecular sieve technique as an analytical tool for the study of protein systems.) | ||||
Children
Sign in to add trainee| Alan D. Frankel | grad student | 1983 | Johns Hopkins (Chemistry Tree) |
| Madeline A. Shea | grad student | 1984 | Johns Hopkins (Chemistry Tree) |
| Ernest S. Burgie | grad student | 2004 | Washington University |
| Bertrand Garcia-Moreno | post-doc | Johns Hopkins (Chemistry Tree) | |
| Dorothy Beckett | post-doc | 1987-1990 | Johns Hopkins (Chemistry Tree) |
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Publications
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| Munro PD, Ackers GK, Shearwin KE. (2016) Aspects of protein-DNA interactions: a review of quantitative thermodynamic theory for modelling synthetic circuits utilising LacI and CI repressors, IPTG and the reporter gene lacZ. Biophysical Reviews. 8: 331-345 |
| Holt JM, Ackers GK. (2012) Kinetic trapping of a key hemoglobin intermediate. Methods in Molecular Biology (Clifton, N.J.). 796: 19-29 |
| Holt JM, Ackers GK. (2009) The Hill coefficient: inadequate resolution of cooperativity in human hemoglobin. Methods in Enzymology. 455: 193-212 |
| Ackers GK, Holt JM. (2006) Asymmetric cooperativity in a symmetric tetramer: human hemoglobin. The Journal of Biological Chemistry. 281: 11441-3 |
| Holt JM, Ackers GK. (2005) Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 2. Stepwise cooperative free energy. Biochemistry. 44: 11939-49 |
| Holt JM, Klinger AL, Yarian CS, et al. (2005) Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 1. Cooperative and noncooperative oxygen binding in Zn-substituted hemoglobin. Biochemistry. 44: 11925-38 |
| Goldbeck RA, Esquerra RM, Kliger DS, et al. (2004) The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 2. Cooperative free energies of (αFeCOβFe)2 and (αFeβFeCO)2 T-state tetramers Biochemistry. 43: 12065-12080 |
| Goldbeck RA, Esquerra RM, Holt JM, et al. (2004) 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: 12048-12064 |
| Ackers GK, Holt JM, Burgie ES, et al. (2004) Analyzing intermediate state cooperativity in hemoglobin. Methods in Enzymology. 379: 3-28 |
| Ackers GK, Dalessio PM, Lew GH, et al. (2002) Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer function. Proceedings of the National Academy of Sciences of the United States of America. 99: 9777-82 |