Protein Folding and Misfolding

1. Front Matter

   Pages i-xvi

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2. Linked Landscapes and Conformational Conversions: How Proteins Fold and Misfold

   • Gareth J. Morgan, Sheena E. Radford

   Pages 1-16

3. A Quantitative Reconstruction of the Amide I Contour in the IR Spectra of Peptides and Proteins: From Structure to Spectrum

   • Joseph W. Brauner, Richard Mendelsohn

   Pages 17-52

4. Millisecond-to-Minute Protein Folding/Misfolding Events Monitored by FTIR Spectroscopy

   • Heinz Fabian, Dieter Naumann

   Pages 53-89

5. Watching Dynamical Events in Protein Folding in the Time Domain from Submilliseconds to Seconds: Continuous-Flow Rapid-Mixing Infrared Spectroscopy

   • Satoshi Takahashi, Tetsunari Kimura

   Pages 91-115

6. High-Pressure Vibrational Spectroscopy Studies of the Folding, Misfolding and Amyloidogenesis of Proteins

   • Roland Winter, Matthias Pühse, Jonas Markgraf

   Pages 117-146

7. Dynamics of α-Helix and β-Sheet Formation Studied by Laser-Induced Temperature-Jump IR Spectroscopy

   • Karin Hauser

   Pages 147-170

8. Light-Triggered Peptide Dynamics

   • Wolfgang Zinth, Josef Wachtveitl

   Pages 171-192

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

   • John E. T. Corrie, Alex Perálvarez-Marín, Andreas Barth

   Pages 193-215

10. Examining Amyloid Structure and Kinetics with 1D and 2D Infrared Spectroscopy and Isotope Labeling

    • Lauren E. Buchanan, Emily B. Dunkelberger, Martin T. Zanni

    Pages 217-237

11. Back Matter

    Pages 239-244

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Infrared spectroscopy is a new and innovative technology to study protein folding/misfolding events in the broad arsenal of techniques conventionally used in this field. The progress in understanding protein folding and misfolding is primarily due to the development of biophysical methods which permit to probe conformational changes with high kinetic and structural resolution. The most commonly used approaches rely on rapid mixing methods to initiate the folding event via a sudden change in solvent conditions. Traditionally, techniques such as fluorescence, circular dichroism or visible absorption are applied to probe the process. In contrast to these techniques, infrared spectroscopy came into play only very recently, and the progress made in this field up to date which now permits to probe folding events over the time scale from picoseconds to minutes has not yet been discussed in a book. The aim of this book is to provide an overview of the developments as seen by some of the main contributors to the field. The chapters are not intended to give exhaustive reviews of the literature but, instead to illustrate examples demonstrating the sort of information, which infrared techniques can provide and how this information can be extracted from the experimental data. By discussing the strengths and limitations of the infrared approaches for the investigation of folding and misfolding mechanisms this book helps the reader to evaluate whether a particular system is appropriate for studies by infrared spectroscopy and which specific advantages the techniques offer to solve specific problems.

• Infrared spectroscopy
• Protein folding/misfolding
• Protein studies
• Time-resolved protein reactions
• Time-resolved spectroscopy
• Protein Structure

• Robert Koch Institut, Berlin, Germany

  Heinz Fabian, Dieter Naumann

Prof. Dr. Dieter Naumann is the head of biomedical spectroscopy at the Robert Koch Institute Berlin

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