Abstract
Previous chapters explain the fundamentals of different spectroscopic techniques that can be used to characterize solution structure of macromolecules and/or cofactors, oxidation and spin states of redox active centers, and molecular interactions. In most cases these are complementary techniques that can bring together a picture of how a macromolecule behaves in solution in respect to substrates, inhibitors, partners in metabolic pathways, etc. This picture is usually representative of a particular equilibrium state such as an enzyme ready state or a cofactor bound to a substrate analogue or inhibitor. However, the description of molecular mechanisms strongly benefits from an additional dimension: time. In this chapter the use of rapid mixing techniques as a tool to acquire spectroscopic data over a time interval and data analysis is discussed.
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Acknowledgements
The Portuguese National Funding Agency FCT-MCTES through Research Grants POCTI/QUI/37413/2001, POCTI/QUI/47273/2002, POCI/QUI/57475/2004, PTDC/QUI/64248/2006, PTDC/QUI/67142/2006, PTDC/SAU-SAP/111482/2009, PTDC/BIA-PRO/111485/2009, and PTDC/OCE-ETA/32567/2017. This work was also supported by Radiation Biology and Biophysics Doctoral Training Programme (RaBBiT, PD/00193/2010); UID/Multi/04378/2019 (UCIBIO); UID/FIS/00068/2013 (CEFITEC).
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Tavares, P., Pereira, A.S. (2019). Fast Kinetics—Stopped-Flow and Rapid Freeze-Quench. In: Pereira, A., Tavares, P., Limão-Vieira, P. (eds) Radiation in Bioanalysis. Bioanalysis, vol 8. Springer, Cham. https://doi.org/10.1007/978-3-030-28247-9_13
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