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7. Cooperative oxygen binding, subunit assembly, and sulfhydryl reaction kinetics of the eight cyanomet intermediate ligation states of human hemoglobin. Doyle ML; Ackers GK Biochemistry; 1992 Nov; 31(45):11182-95. PubMed ID: 1445857 [TBL] [Abstract][Full Text] [Related]
8. The molecular code for hemoglobin allostery revealed by linking the thermodynamics and kinetics of quaternary structural change. 1. Microstate linear free energy relations. Goldbeck RA; Esquerra RM; Holt JM; Ackers GK; Kliger DS Biochemistry; 2004 Sep; 43(38):12048-64. PubMed ID: 15379545 [TBL] [Abstract][Full Text] [Related]
9. Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 1. Cooperative and noncooperative oxygen binding in Zn-substituted hemoglobin. Holt JM; Klinger AL; Yarian CS; Keelara V; Ackers GK Biochemistry; 2005 Sep; 44(36):11925-38. PubMed ID: 16142891 [TBL] [Abstract][Full Text] [Related]
10. Asymmetric distribution of cooperativity in the binding cascade of normal human hemoglobin. 2. Stepwise cooperative free energy. Holt JM; Ackers GK Biochemistry; 2005 Sep; 44(36):11939-49. PubMed ID: 16142892 [TBL] [Abstract][Full Text] [Related]
12. 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 tetramers. Goldbeck RA; Esquerra RM; Kliger DS; Holt JM; Ackers GK Biochemistry; 2004 Sep; 43(38):12065-80. PubMed ID: 15379546 [TBL] [Abstract][Full Text] [Related]
13. Hemoglobin/O2 systems: mechanistic discrimination based on Ackers' model. Czerlinski G; Levin R; Ypma T Physiol Chem Phys Med NMR; 2002; 34(1):17-42. PubMed ID: 12403273 [TBL] [Abstract][Full Text] [Related]
14. Single-site modifications of half-ligated hemoglobin reveal autonomous dimer cooperativity within a quaternary T tetramer. LiCata VJ; Dalessio PM; Ackers GK Proteins; 1993 Nov; 17(3):279-96. PubMed ID: 8272426 [TBL] [Abstract][Full Text] [Related]
15. Protein's native state stability in a chemically induced denaturation mechanism. Olivares-Quiroz L; Garcia-Colin LS J Theor Biol; 2007 May; 246(2):214-24. PubMed ID: 17306831 [TBL] [Abstract][Full Text] [Related]
16. Oxygen binding by single crystals of hemoglobin: the problem of cooperativity and inequivalence of alpha and beta subunits. Bettati S; Mozzarelli A; Rossi GL; Tsuneshige A; Yonetani T; Eaton WA; Henry ER Proteins; 1996 Aug; 25(4):425-37. PubMed ID: 8865338 [TBL] [Abstract][Full Text] [Related]
17. An allosteric theory for hemoglobin incorporating asymmetric states to test the putative molecular code for cooperativity. Edelstein SJ J Mol Biol; 1996 Apr; 257(4):737-44. PubMed ID: 8636978 [TBL] [Abstract][Full Text] [Related]
18. The energetics of ligand-linked subunit assembly in hemoglobin require a third allosteric structure. Ackers GK Biophys Chem; 1990 Aug; 37(1-3):371-82. PubMed ID: 2285798 [TBL] [Abstract][Full Text] [Related]
19. Confirmation of a unique intra-dimer cooperativity in the human hemoglobin alpha(1)beta(1)half-oxygenated intermediate supports the symmetry rule model of allosteric regulation. Ackers GK; Holt JM; Huang Y; Grinkova Y; Klinger AL; Denisov I Proteins; 2000; Suppl 4():23-43. PubMed ID: 11013398 [TBL] [Abstract][Full Text] [Related]
20. Exhaustive mutagenesis in silico: multicoordinate free energy calculations on proteins and peptides. Pitera JW; Kollman PA Proteins; 2000 Nov; 41(3):385-97. PubMed ID: 11025549 [TBL] [Abstract][Full Text] [Related] [Next] [New Search]