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Time-Resolved FTIR Spectroscopy of pH-Induced Aggregation of Peptides

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Protein Folding and Misfolding

Part of the book series: Biological and Medical Physics, Biomedical Engineering ((BIOMEDICAL))

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Abstract

Reaction-induced infrared difference spectroscopy is a sensitive method to detect absorbance changes that accompany biomolecular reactions, even if they are very small. One of the ways to trigger reactions in the infrared cuvette is the use of caged compounds, photosensitive molecules that release a desired effector molecule when irradiated with near-UV light, and experiments with caged nucleotides and the sarcoplasmic reticulum Ca2+-ATPase are used to introduce the methodology. A caged sulfate, which can be used to rapidly acidify protein or peptide samples in order to induce unfolding and misfolding, is discussed in detail. Applications described are the partial unfolding of myoglobin and the aggregation of the Alzheimers peptide.

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Authors and Affiliations

  1. MRC National Institute for Medical Research, The Ridgeway Mill Hill, London, NW7 1AA, UK

    John E. T. Corrie

  2. Harvard University, 52 Oxford Street, NorthWest Building, Cambridge, MA, 02138, USA

    Alex Perálvarez-Marín

  3. Department of Biochemistry and Biophysics, Arrhenius Laboratories, Stockholm University, 10691, Stockholm, Sweden

    Andreas Barth

Authors
  1. John E. T. Corrie
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  2. Alex Perálvarez-Marín
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  3. Andreas Barth
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Correspondence to Andreas Barth .

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Editors and Affiliations

  1. Robert Koch Institut, Nordufer 20, Berlin, 13353, Germany

    Heinz Fabian

  2. Robert Koch Institut, Nordufer 20, Berlin, 13353, Germany

    Dieter Naumann

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Corrie, J.E.T., Perálvarez-Marín, A., Barth, A. (2012). Time-Resolved FTIR Spectroscopy of pH-Induced Aggregation of Peptides. In: Fabian, H., Naumann, D. (eds) Protein Folding and Misfolding. Biological and Medical Physics, Biomedical Engineering. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-22230-6_8

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  • DOI: https://doi.org/10.1007/978-3-642-22230-6_8

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