Temperature jump kinetic study of the stability of apo-calmodulin

Biophysical Chemistry

Volumn 101-102, Issue , 2002, Pages 553-564

  Rabl, Carl Roland ^a   Martin, Stephen R ^b   Neumann, Eberhard ^a   Bayley, Peter M ^b  

^a BIELEFELD UNIVERSITY   (Germany)

^b NATIONAL INSTITUTE FOR MEDICAL RESEARCH   (United Kingdom)

Author keywords

Calmodulin; Protein dynamics; Protein folding; Relaxation kinetics; Temperature (T) jump

Indexed keywords

CALCIUM ION; CALMODULIN; META TYROSINE; RECOMBINANT PROTEIN;

ARTICLE; CONTROLLED STUDY; DROSOPHILA; ENERGY; IONIC STRENGTH; KINETICS; MOLECULAR DYNAMICS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FOLDING; PROTEIN STABILITY; SPECTROMETRY; TEMPERATURE DEPENDENCE; TIME; ANIMAL; CHEMISTRY; OSMOLARITY; TEMPERATURE; THERMODYNAMICS;

ANIMALS; CALMODULIN; DROSOPHILA; KINETICS; OSMOLAR CONCENTRATION; RECOMBINANT PROTEINS; TEMPERATURE; THERMODYNAMICS;

EID: 0037058908     PISSN: 03014622     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0301-4622(02)00150-3     Document Type: Article

References (41)

1. Crivici A., Ikura M. Molecular and structural basis of target recognition by calmodulin. Annu. Rev. Biophys. Biomol. Struct. 24:1995;85-116.
2. Rhoads A.R., Friedberg F. Sequence motifs for calmodulin recognition. FASEB J. 11:1997;331-340.
3. Bähler M., Rhoads A. Calmodulin signalling via the IQ motif'. FEBS Lett. 513:2002;107-113.
4. Peng Z.-Y., Wu L.C. Autonomous protein folding units. Adv. Protein Chem. 53:2000;1-47.
5. Chen B.-L., Baase W.A., Schellman J.A. Low-temperature unfolding of a mutant of phage T4 lysozyme. 2. Kinetic investigations. Biochemistry. 28:1989;691-699.
6. Schellman J.A. The thermodynamic stability of proteins. Annu. Rev. Biophys. Biophys. Chem. 16:1987;115-137.
7. Becktel W.J., Schellman J.A. Protein stability curves. Biopolymers. 26:1987;1859-1877.
8. Jackson S.E. How do small single-domain proteins fold? Folding Des. 3:1998;R81-R91.
9. Pace C.N. Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol. 131:1986;266-280.
10. Fersht R. Structure and Mechanism in Protein Science: A Guide to Enzyme Catalysis and Protein Folding. 1998;W.H. Freeman, New York.
11. Masino L., Martin S.R., Bayley P.M. Ligand binding and thermodynamic stability of a multidomain protein, calmodulin. Protein Sci. 9:2000;1519-1529.
12. Schellman J.A. Solvent denaturation. Biopolymers. 17:1978;1305-1322.
13. Browne J.P., Strom M., Martin S.R., Bayley P.M. The role of β-sheet interactions in domain stability, folding, and target recognition reactions of calmodulin. Biochemistry. 36:1997;9550-9561.
14. Schellman J.A. Macromolecular binding. Biopolymers. 14:1975;999-1018.
15. 2+-dependent interactions of calmodulin with target sequences. Protein Sci. 9:2000;2477-2488.
16. Kuboniwa H., Tjandra N., Grzesiek S., Ren H., Klee C.B., Bax A. Solution structure of calcium-free calmodulin. Nat. Struct. Biol. 2:1995;768-776.
17. Zhang M., Tanaka T., Ikura M. Calcium-induced conformational transition revealed by the solution structure of apo-calmodulin. Nat. Struct. Biol. 2:1995;758-767.
18. Finn B.E., Evenäs L., Drakenberg T., Waltho J.P., Thulin E., Forsén S. Calcium-induced structural changes and domain autonomy in calmodulin. Nat. Struct. Biol. 2:1995;777-783.
19. 15N-NMR relaxation measurements. Eur. J. Biochem. 230:1995;1014-1024.
20. Urbauer J.L., Short J.H., Dow L.K., Wand A.J. Structural analysis of a novel interaction by calmodulin: high-affinity binding of a peptide in the absence of calcium. Biochemistry. 34:1995;8099-8109.
21. Bayley P.M. Stopped-flow circular dichroism techniques: scope and limitations. Prog. Biophys. 37:1981;149-180.
22. Kuwajima K., Sakuraoka A., Fueki S., Yoneyama M., Sugai S. Folding of carp parvalbumin studied by equilibrium and kinetic circular dichroism spectra. Biochemistry. 27:1988;7419-7428.
23. Roder H., Shastry M.C.R. Methods for exploring early events in protein folding. Curr. Opin. Struct. Biol. 9:1999;620-626.
24. Eigen M., DeMaeyer L. Theoretical basis of relaxation spectrometry. Weissberger A., Hammes G.G. Techniques of Chemistry, vol. VI. 3rd ed. 1974;63-146 Wiley, New York.
25. Hofrichter J. Laser temperature-jump methods for studying folding dynamics. Methods Mol. Biol. 168:2001;159-191.
26. Jacob M., Holtermann G., Perl D., et al. Microsecond folding of the cold shock protein measured by a pressure-jump technique'. Biochemistry. 38:1999;2882-2891.
27. Tsalkova T.N., Privalov P.L. Thermodynamic study of domain organisation in troponin C and calmodulin. J. Mol. Biol. 181:1985;533-544.
28. Rigler R., Rabl C.R., Jovin T.M. A temperature-jump apparatus for fluorescence measurements. Rev. Sci. Instrum. 45:1974;580-588.
29. Rabl C.R. Kinetik und Reaktionsmechanismus des biologischen Calcium-Indikators Arsenazo III. PhD Thesis. 1985;University of Konstanz, Germany.
30. Rabl C.R. Relaxationsmesstechnik. Rehm H.J. Technische Biochemie, Dechema Monographies, vol. 71. 1973;187-205 Verlag Chemie, Weinheim.
31. Mihalyi E. Numerical values of the absorbance of the aromatic amino acids in acid, neutral, and alkaline solutions. J. Chem. Eng. Data. 13:1968;179-182.
32. Sorensen B.R., Shea M.A. Interactions between domains of apo calmodulin alter calcium binding and stability. Biochemistry. 37:1998;4244-4253.
33. Robertson A.D., Murphy K.P. Protein structure and the energetics of protein stability. Chem. Rev. 97:1997;1251-1267.
34. Schindler T., Schmid F.X. Thermodynamic properties of an extremely rapid protein folding reaction. Biochemistry. 35:1996;16833-16842.
35. 5 using equilibrium and kinetic fluorescence measurements. Biochemistry. 38:1999;9533-9540.
36. Segawa S.-I., Sugihara M. Characterisation of the transition state of lysozyme unfolding. I. Effect of protein-solvent interactions in the transition state. Biopolymers. 23:1984;2472-2488.
37. Mayor U., Johnson C.M., Daggett V., Fersht A.R. Protein folding and unfolding in microseconds to nanoseconds by experiment and simulation. Proc. Natl. Acad. Sci. USA. 97:2000;13518-13522.
38. 2+-bound calmodulin: an analysis of disorder and implications for functionally relevant plasticity. J. Mol. Biol. 301:2000;1237-1256.
39. 15N relaxation using inverse detected two-dimensional NMR spectroscopy. The central helix is flexible. Biochemistry. 31:1992;5269-5278.
40. Rabl C.R. High-resolution temperature-jump measurements using cooling correction. Gettins W.J., Wyn-Jones E. Techniques and Applications of Fast Reactions in Solution. 1979;77-82 Reidel, Dordrecht.
41. Phe (yeast) as studied by the fluorescence of the Y-base and of formycin. Biophys. Chem. 3:1975;275-289.