calmodulin and troponin C. Biochemistry
27:909–915
7. Finn BE, Evenas J, Drakenberg T et al (1995)
Calcium-induced structural changes and
domain autonomy in calmodulin. Nat Struct
Biol 2:777–783
8. Barman TE, Bellamy SR, Gutfreund H et al
(2006) The identification of chemical intermediates in enzyme catalysis by the rapid
quench-flow technique. Cell Mol Life Sci
63:2571–2583
9. Shastry MCR, Luck SD, Roder H (1998) A
continuous-flow capillary mixer to monitor
reactions on the microsecond time scale. Biophys J 74:2714–2721
10. Martin SR, Schilstra MJ (2013) Rapid mixing
kinetic techniques. In: Williams M, Daviter T
(eds) Protein-ligand interactions. Methods in
molecular biology (methods and protocols),
vol 1008. Humana Press, Totowa, NJ, pp
p119–p138
11. Eccleston JF, Martin SR, Schilstra MJ (2008)
Rapid kinetic techniques. Methods Cell Biol
84:445–477
12. Browne JP, Strom M, Martin SR et al (1997)
The role of β-sheet interactions in domain stability, folding, and target recognition reactions
of calmodulin. Biochemistry 36:9550–9561
13. Clapperton JA, Martin SR, Smerdon SJ et al
(2002) Structure of the complex of calmodulin
with the target sequence of calmodulindependent protein kinase I: studies of the
kinase activation mechanism. Biochemistry
41:14669–14479
14. Martin SR, Andersson-Teleman A, Bayley PM
et al (1985) Kinetics of calcium dissociation
from calmodulin and its tryptic fragments. A
Quin 2 stopped‑flow fluorescence study reveals
a two‑domain structure. Eur J Biochem
151:543–550
15. Halford SE (1971) Escherichia coli alkaline
phosphatase. An analysis of transient kinetics.
Biochem J 125:319–327
16. De La Cruz EM, Ostap EM, Sweeney HL
(2001) Kinetic mechanism and regulation of
myosin VI. J Biol Chem 276:32373–32381
17. Eccleston JF, Hutchinson JP, White HD
(2001) Stopped-flow techniques. In: Harding
SE, Chowdhry BZ (eds) Protein-ligand interactions: structure and spectroscopy. Oxford
University Press, Oxford
18. De La Cruz EM, Wells AL, Rosenfeld SS et al
(1999) The kinetic mechanism of myosin
V. PNAS 96:13726–13731
19. Eccleston JF, Petrovic A, Davis CT et al (2006)
The kinetic mechanism of the SufC ATPase:
the cleavage step is accelerated by SufB. J Biol
Chem 281:8371–8378
20. Kuzmic P (1996) Program DYNAFIT for the
analysis of enzyme kinetic data: application to
HIV proteinase. Anal Biochem 237:260–273
21. Schilstra MJ, Martin SR, Keating SM (2008)
Methods for simulating the dynamics of complex biological processes. Methods Cell Biol
84:807–842
22. Woodward SKA, Eccleston JF, Geeves MA
(1991) Kinetics of the interaction of 2
0 (3
0 )-O(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1:
characterization of two acto.S1.ADP complexes. Biochemistry 30:422–430
23. Johnson ML (2008) Nonlinear least-squares
fitting
methods. Methods Cell Biol
84:781–805
24. Press WH, Teukolsky BP, Vetterling WT et al
(1990) Numerical recipes. The art of scientific
computing. Cambridge University Press,
Cambridge
104
Stephen R. Martin and Maria J. Schilstra
27:909–915
7. Finn BE, Evenas J, Drakenberg T et al (1995)
Calcium-induced structural changes and
domain autonomy in calmodulin. Nat Struct
Biol 2:777–783
8. Barman TE, Bellamy SR, Gutfreund H et al
(2006) The identification of chemical intermediates in enzyme catalysis by the rapid
quench-flow technique. Cell Mol Life Sci
63:2571–2583
9. Shastry MCR, Luck SD, Roder H (1998) A
continuous-flow capillary mixer to monitor
reactions on the microsecond time scale. Biophys J 74:2714–2721
10. Martin SR, Schilstra MJ (2013) Rapid mixing
kinetic techniques. In: Williams M, Daviter T
(eds) Protein-ligand interactions. Methods in
molecular biology (methods and protocols),
vol 1008. Humana Press, Totowa, NJ, pp
p119–p138
11. Eccleston JF, Martin SR, Schilstra MJ (2008)
Rapid kinetic techniques. Methods Cell Biol
84:445–477
12. Browne JP, Strom M, Martin SR et al (1997)
The role of β-sheet interactions in domain stability, folding, and target recognition reactions
of calmodulin. Biochemistry 36:9550–9561
13. Clapperton JA, Martin SR, Smerdon SJ et al
(2002) Structure of the complex of calmodulin
with the target sequence of calmodulindependent protein kinase I: studies of the
kinase activation mechanism. Biochemistry
41:14669–14479
14. Martin SR, Andersson-Teleman A, Bayley PM
et al (1985) Kinetics of calcium dissociation
from calmodulin and its tryptic fragments. A
Quin 2 stopped‑flow fluorescence study reveals
a two‑domain structure. Eur J Biochem
151:543–550
15. Halford SE (1971) Escherichia coli alkaline
phosphatase. An analysis of transient kinetics.
Biochem J 125:319–327
16. De La Cruz EM, Ostap EM, Sweeney HL
(2001) Kinetic mechanism and regulation of
myosin VI. J Biol Chem 276:32373–32381
17. Eccleston JF, Hutchinson JP, White HD
(2001) Stopped-flow techniques. In: Harding
SE, Chowdhry BZ (eds) Protein-ligand interactions: structure and spectroscopy. Oxford
University Press, Oxford
18. De La Cruz EM, Wells AL, Rosenfeld SS et al
(1999) The kinetic mechanism of myosin
V. PNAS 96:13726–13731
19. Eccleston JF, Petrovic A, Davis CT et al (2006)
The kinetic mechanism of the SufC ATPase:
the cleavage step is accelerated by SufB. J Biol
Chem 281:8371–8378
20. Kuzmic P (1996) Program DYNAFIT for the
analysis of enzyme kinetic data: application to
HIV proteinase. Anal Biochem 237:260–273
21. Schilstra MJ, Martin SR, Keating SM (2008)
Methods for simulating the dynamics of complex biological processes. Methods Cell Biol
84:807–842
22. Woodward SKA, Eccleston JF, Geeves MA
(1991) Kinetics of the interaction of 2
0 (3
0 )-O(N-methylanthraniloyl)-ATP with myosin subfragment 1 and actomyosin subfragment 1:
characterization of two acto.S1.ADP complexes. Biochemistry 30:422–430
23. Johnson ML (2008) Nonlinear least-squares
fitting
methods. Methods Cell Biol
84:781–805
24. Press WH, Teukolsky BP, Vetterling WT et al
(1990) Numerical recipes. The art of scientific
computing. Cambridge University Press,
Cambridge
104
Stephen R. Martin and Maria J. Schilstra