On the relationship between the hill coefficients for steady-state and transient kinetic data: A criterion for concerted transitions in allosteric proteins

Bulletin of Mathematical Biology

Volumn 62, Issue 2, 2000, Pages 241-246

  Horovitz, Amnon ^a   Yifrach, Ofer ^a  

^a WEIZMANN INSTITUTE OF SCIENCE   (Israel)

Author keywords

[No Author keywords available]

Indexed keywords

CHAPERONIN;

ALLOSTERISM; ARTICLE; LIGAND BINDING; MATHEMATICAL MODEL; PROTEIN ANALYSIS; PROTEIN CONFORMATION; STEADY STATE;

EID: 0033782257     PISSN: 00928240     EISSN: None     Source Type: Journal    
DOI: 10.1006/bulm.1999.0150     Document Type: Article

References (10)

1. Kinetics of reaction control and information transfer in enzymes and nucleic acids
2. GroEL-mediated protein folding
3. Kinetic cooperativity in the concerted model for allosteric enzymes
4. Chemical relaxation spectra: Calculation of relaxation times for complex mechanisms
5. The possible effects of the aggregation of the molecules of haemoglobin on its dissociation curves
6. Structural aspects of GroEL function
7. Comparison of experimental binding data and theoretical models in proteins containing subunits
8. On the nature of allosteric transitions: A plausible model
9. Mechanisms of co-operativity and allosteric regulation in proteins
10. Mapping the transition state of the allosteric pathway of GroEL by protein engineering