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Jo M Holt

Showing results (1-10 of 11) with videos related to

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Methods in Molecular Biology (Clifton, N.J.)|November 5, 2011
Kinetic trapping of a key hemoglobin intermediateJo M Holt, Gary K Ackers
The Journal of Biological Chemistry|January 21, 2006
Asymmetric cooperativity in a symmetric tetramer: human hemoglobinGary K Ackers, Jo M Holt
Methods in Enzymology|March 18, 2009
The Hill coefficient: inadequate resolution of cooperativity in human hemoglobinJo M Holt, Gary K Ackers
Biochemistry|September 7, 2005
Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 2. Stepwise cooperative free energyJo M Holt, Gary K Ackers
Methods in Enzymology|March 18, 2009
Biothermodynamics, Part A. PrefaceMichael L Johnson, Jo M Holt, Gary K Ackers
Methods in Enzymology|March 31, 2004
Analyzing intermediate state cooperativity in hemoglobinGary K Ackers, Jo M Holt, E Sethe Burgie, et al.
Biochemistry|September 7, 2005
Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 1. Cooperative and noncooperative oxygen binding in Zn-substituted hemoglobinJo M Holt, Alexandra L Klinger, Connie S Yarian, et al.
Biochemistry|September 24, 2004
The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 2. Cooperative free energies of (alphaFeCObetaFe)2 and (alphaFebetaFeCO)2 T-state tetramersRobert A Goldbeck, Raymond M Esquerra, David S Kliger, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 18, 2002
Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer functionGary K Ackers, Paula M Dalessio, George H Lew, et al.
Biochemistry|September 24, 2004
The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 1. Microstate linear free energy relationsRobert A Goldbeck, Raymond M Esquerra, Jo M Holt, et al.
Pageof 2

Showing results (1-10 of 11) with videos related to

Sort By:
Pageof 2
Methods in Molecular Biology (Clifton, N.J.)|November 5, 2011
Kinetic trapping of a key hemoglobin intermediateJo M Holt, Gary K Ackers
The Journal of Biological Chemistry|January 21, 2006
Asymmetric cooperativity in a symmetric tetramer: human hemoglobinGary K Ackers, Jo M Holt
Methods in Enzymology|March 18, 2009
The Hill coefficient: inadequate resolution of cooperativity in human hemoglobinJo M Holt, Gary K Ackers
Biochemistry|September 7, 2005
Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 2. Stepwise cooperative free energyJo M Holt, Gary K Ackers
Methods in Enzymology|March 18, 2009
Biothermodynamics, Part A. PrefaceMichael L Johnson, Jo M Holt, Gary K Ackers
Methods in Enzymology|March 31, 2004
Analyzing intermediate state cooperativity in hemoglobinGary K Ackers, Jo M Holt, E Sethe Burgie, et al.
Biochemistry|September 7, 2005
Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 1. Cooperative and noncooperative oxygen binding in Zn-substituted hemoglobinJo M Holt, Alexandra L Klinger, Connie S Yarian, et al.
Biochemistry|September 24, 2004
The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 2. Cooperative free energies of (alphaFeCObetaFe)2 and (alphaFebetaFeCO)2 T-state tetramersRobert A Goldbeck, Raymond M Esquerra, David S Kliger, et al.
Proceedings of the National Academy of Sciences of the United States of America|July 18, 2002
Single residue modification of only one dimer within the hemoglobin tetramer reveals autonomous dimer functionGary K Ackers, Paula M Dalessio, George H Lew, et al.
Biochemistry|September 24, 2004
The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 1. Microstate linear free energy relationsRobert A Goldbeck, Raymond M Esquerra, Jo M Holt, et al.
Pageof 2