4.6 Article

Steady-state fluorescence quenching applications for studying protein structure and dynamics

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ELSEVIER SCIENCE SA
DOI: 10.1016/j.jphotobiol.2005.12.017

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fluorescence quenching; protein structure; FRET; tryptophan fluorescence

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Fluorescence quenching methods are useful to obtain information about the conformational and/or dynamic changes of proteins in complex macromolecular systems. In this review steady-state methods are described and the data interpretation is thoroughly discussed. As a special case of fluorescence quenching mechanism, fluorescence resonance energy transfer (FRET) phenomenon is also presented. Application of a FRET based method to characterize the temperature dependence of the flexibility of protein matrix is clearly demonstrated. (c) 2006 Elsevier B.V. All rights reserved.

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