Phase diagrams: A graphical representation of linkage relations

Journal of Molecular Biology

Volumn 328, Issue 1, 2003, Pages 255-271

  Rösgen, Jörg ^a   Hinz, Hans Jürgen ^a  

^a UNIVERSITY OF MÜNSTER   (Germany)

Author keywords

Denaturation; Ligand binding; Linkage; Phase transition; Statistical thermodynamics

Indexed keywords

ACRYLIC ACID DERIVATIVE; BETA INDOLE ACRYLIC ACID; LIGAND; LIPOCORTIN 1; METALLO BETA LACTAMASE; NUCLEASE; PENICILLINASE; RIBONUCLEASE A; UNCLASSIFIED DRUG; ZINC;

ANALYTIC METHOD; ARTICLE; BINDING AFFINITY; CHEMICAL REACTION; MACROMOLECULE; PH; PHASE DIAGRAM; PRESSURE; PRIORITY JOURNAL; STAPHYLOCOCCUS; STOICHIOMETRY; TEMPERATURE;

EID: 0037453260     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0022-2836(03)00246-8     Document Type: Article

References (35)

1. Wyman J., Gill S.J. Binding and Linkage. 1990;University Science Books, Mill Valley, CA.
2. Hill T.L. Thermodynamics of Small Systems, Part 1. 1963;W.A. Benjamin, New York.
3. Rösgen J., Hinz H.-J. Statistical thermodynamic treatment of conformational transitions of monomeric and oligomeric proteins. Phys. Chem. Chem. Phys. 1:1999;2327-2333.
4. Balian R. From Microphysics to Macrophysics. 1990;Springer, Berlin.
5. Wyman J. Linked functions and reciprocal effects in hemoglobin: a second look. Advan. Protein Chem. 19:1964;223-286.
6. Lumry R., Biltonen R. Validity of the "Two-State" hypothesis for conformational transitions of proteins. Biopolymers. 4:1966;917-944.
7. Dixon M., Webb E.C. Enzymes. 1964;Academic press, New York.
8. Michaelis L. Die Wasserstoffionenkonzentration. 1922;Springer, Berlin.
9. Kavanoor M., Eftink M.R. Characterisation of the role of side-chain interactions in the binding of ligands to apo trp repressor: pH dependence studies. Biophys. Chem. 66:1997;43-55.
10. Rösgen J., Hinz H.-J. Folding energetics of ligand binding proteins I. Theoretical model. J. Mol. Biol. 306:2001;809-824.
11. Chalikian T., Völker J., Anafi D., Breslauer K.J. The native and heat-induced denatured states of α-chymotrypsinogen A: thermodynamic and spectroscopic studies. J. Mol. Biol. 274:1997;237-252.
12. 2+ to annexin I. J. Mol. Biol. 306:2001;825-835.
13. Weng R., Luecke H., Song I., Kang D.S., Kim S.-H., Huber R. Crystal structure of human annexin I at 2.5 Å resolution. Protein Sci. 2:1993;448-458.
14. Rosengarth A., Gerke V., Luecke H. X-ray structure of full-length annexin I and implications form membrane aggregation. J. Mol. Biol. 306:2001;489-498.
15. Brandts J.F., Lin L.-N. Study of strong to ultratight protein interactions using differential scanning calorimetry. Biochemistry. 29:1990;6927-6940.
16. Rösgen J., Hinz H.-J. The heat capacity paradox of ligand binding proteins: reconciliation of the microscopic and macroscopic world. Biophys. Chem. 96:2002;109-116.
17. Robert C.H., Gill S.J., Wyman J. Quantitative analysis of linkage in macromolecules when one ligand is present in limited total quantity. Biochemistry. 27:1988;6829-6835.
18. Robert C.H., Colosimo A., Gill S.J. Allosteric formulation of thermal transitions in macromolecules including effects of ligand binding and oligomerization. Biopolymers. 28:1989;1705-1729.
19. Shrake A., Ross P.D. Ligand-induced biphasic protein denaturation. J. Biol. Chem. 265:1990;5055-5059.
20. Straume M., Freire E. Two-dimensional differential scanning calorimetry: simultaneous resolution of intrinsic protein structural energetics and ligand binding interactions by global linkage analysis. Anal. Biochem. 203:1992;259-268.
21. Hernandez Valladares M., Felici A., Weber G., Adolph H.W., Zeppezauer M., et al. Zn(II) dependence of the Aeromaonas hydrophila AE036 metallo-β-lactamase activity and stability. Biochemistry. 36:1997;11534-11541.
22. Heremans K., Smeller L. Protein structure and dynamics at high pressure. Biochim. Biophys. Acta. 1386:1998;353-370.
23. Smeller L. Pressure-temperature phase diagrams of biomolecules. Biochim. Biophys. Acta. 1595:2002;11-29.
24. Zhang J., Xiangdong P., Jonas A., Jonas J. NMR study of the cold, heat and pressure unfolding of ribonuclease A. Biochemistry. 34:1995;8631-8641.
25. 1H NMR. J. Mol. Biol. 298:2000;293-302.
26. Dubins D.N., Lee A., Macgregor R.B., Chalikian T.V. On the stability of double stranded nucleic acids. J. Am. Chem. Soc. 123:2001;9254-9259.
27. Becktel, Schellman. Protein stability curves. Biopolymers. 26:1987;1859-1877.
28. Rösgen J., Hinz H.-J. Response functions of proteins. Biophys. Chem. 83:2000;61-71.
29. Hinz H.-J., Vogl T., Meyer R. An alternative interpretation of the heat capacity changes associated with protein unfolding. Biophys. Chem. 52:1994;275-285.
30. Brandts J.F., Oliveira R.J., Westort C. Thermodynamics of ribonuclease A. Biochemistry. 9:1970;1038-1047.
31. Lin L.-N., Brandts J.F., Brandts M., Plotnikov V. Determination of the volumetric properties of proteins and other solutes using pressure perturbation calorimetry. Anal. Biochem. 302:2002;144-160.
32. Høiland H. Partial molar volumes of biochemical model compounds in aqueous solution. Hinz H.-J. Thermodynamic Data for Biochemistry and Biotechnology. 1986;Springer, Berlin.
33. Høiland H. Partial molar compressibilities of organic solutes in water. Hinz H.-J. Thermodynamic Data for Biochemistry and Biotechnology. 1986;Springer, Berlin.
34. Taulier N., Chalikian T.V. Compressibility of protein transitions. Biochim. Biophys. Acta. 1595:2002;48-70.
35. Seemann H., Winter R., Royer C.A. Volume expansion and isothermal compressibility changes associated with temperature and pressure unfolding of staphylococcal nuclease. J. Mol. Biol. 307:2001;1091-1102.