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Tracking Molecular Dynamics of Flavoproteins with Time-Resolved Fluorescence Spectroscopy

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New Trends in Fluorescence Spectroscopy

Part of the book series: Springer Series on Fluorescence ((SS FLUOR,volume 1))

Abstract

The intrinsic fluorescence of tryptophan containing proteins is nowadays commonly used to study the physical and dynamic properties of this prominent class of biomacromolecules [1–5]. Although tryptophan fluorescence experiments have provided detailed insight in many protein systems, the applicability of the technique is strongly dependent on the number and position of the tryptophan residues, as well as on the specific research objective Reason for this is the well-known complexity of the photophysical properties of the indole ring. Due to the degeneracy of energy levels in the excited state (1 L A and 1 L B) the observed nonexponential fluorescence decays are rather rule than exception, even in proteins that contain only one tryptophan in a rigid protein environment. In addition, fast depolarization of the fluorescence originating from interconversion between these two states complicates the interpretation of time— resolved fluorescence anisotropy measurements [6]. Particularly for the investigation of dynamic events such as protein motions, these fluorescence characteristics of the indole moietv prove a serious obstacle.

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  1. P. A. W. van den Berg
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  2. A. J. W. G. Visser
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Editors and Affiliations

  1. Conservatoire National des Arts et Métiers, Laboratoire de Chimie Général, 292 rue Saint-Martin, 75141, Paris Cedex 03, France

    Bernard Valeur

  2. Ecole Normale Supérieure de Cachan, 61 Av. du Président Wilson, 94235, Cachan Cedex, France

    Jean-Claude Brochon

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van den Berg, P.A.W., Visser, A.J.W.G. (2001). Tracking Molecular Dynamics of Flavoproteins with Time-Resolved Fluorescence Spectroscopy. In: Valeur, B., Brochon, JC. (eds) New Trends in Fluorescence Spectroscopy. Springer Series on Fluorescence, vol 1. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-56853-4_22

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