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Fluorescence Spectroscopy-Based Methods to Study Protein Folding Dynamics

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Protein Folding Dynamics and Stability

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Abstract

The biological function of a protein is characterised by its three-dimensional conformation and encoded by its amino acid sequence. Tremendous effort has been devoted to understanding the mechanism of protein folding and how the amino acid sequences encode the correct functional conformation of a protein. Fluorescence-based methods, such as time-resolved spectroscopy, fluorescence correlation spectroscopy, or labelling of the proteins by external fluorescent dyes, have been employed to understand the protein folding dynamics. Herein, we describe recent fluorescence spectroscopy-based techniques used to study the conformational dynamics of a protein. Furthermore, these techniques are commonly available in most research laboratories and are used to study the protein–protein, protein–DNA, and protein–ligand interactions. We focus on the extrinsic fluorescent dyes to characterise the folding intermediates and detect the amyloid fibril aggregation in Alzheimer’s and Parkinson’s diseases.

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Authors and Affiliations

  1. Department of Internal Medicine, UT Southwestern Medical Center, Dallas, TX, USA

    Ritesh Kumar

  2. Molecular and Structural Biophysics Laboratory, Department of Biochemistry, North-Eastern Hill University, Shillong, India

    Timir Tripathi

  3. Department of Biotechnology, National Institute of Technology Warangal, Warangal, India

    Prakash Saudagar

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  1. Ritesh Kumar
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  2. Timir Tripathi
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Correspondence to Prakash Saudagar .

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Editors and Affiliations

  1. Department of Biotechnology, National Institute of Technology, Warangal, Telangana, India

    Prakash Saudagar

  2. Department of Biochemistry, North-Eastern Hill University, Shillong, Meghalaya, India

    Timir Tripathi

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Kumar, R., Tripathi, T., Saudagar, P. (2023). Fluorescence Spectroscopy-Based Methods to Study Protein Folding Dynamics. In: Saudagar, P., Tripathi, T. (eds) Protein Folding Dynamics and Stability. Springer, Singapore. https://doi.org/10.1007/978-981-99-2079-2_2

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