Protein Folding Misfolding and Disease Methods and Protocols 1st Edition by Andrew F Hill, Kevin J Barnham, Stephen P Bottomley, Roberto Cappai ISBN 1603272216 9781603272216

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ISBN 10: 1603272216 
ISBN 13: 9781603272216
Author: Andrew F Hill, Kevin J Barnham, Stephen P Bottomley, Roberto Cappai

Protein misfolding is a key feature of many disorders in humans, given that over twenty proteins are known to misfold and cause disease. In Protein Folding, Misfolding, and Disease: Methods and Protocols, experts in the field present a collection of current methods for studying the analysis of protein folding and misfolding, featuring strategies for expressing and refolding recombinant proteins which can then be utilized in subsequent experiments. This detailed volume also covers methods for analyzing the formation of amyloid, protocols for determining the size and structure of native and misfolded proteins, as well as specific examples of where misfolded proteins can be examined using state-of –the-art technologies. Written in the highly successful Methods in Molecular Biology™ series format, chapters contain introductions to their respective topics, lists of the necessary materials and reagents, step-by-step, readily reproducible laboratory protocols, and key tips on troubleshooting and avoiding known pitfalls.

Up to date and authoritative, Protein Folding, Misfolding, and Disease: Methods and Protocols offers researchers the tools necessary to move ahead in this vital field.

Protein Folding Misfolding and Disease Methods and Protocols 1st Table of contents:

Part I: Introduction to Protein Folding and Misfolding

1. Introduction to Protein Folding

   • Overview of protein folding principles.
   • The folding pathway and its thermodynamics.
   • The role of chaperones in protein folding.

2. Protein Misfolding and Disease

   • The connection between protein misfolding and diseases like Alzheimer’s, Parkinson’s, Huntington’s, and cystic fibrosis.
   • Mechanisms of toxicity associated with misfolded proteins.
   • Prion diseases and the propagation of misfolded proteins.

Part II: Experimental Methods for Studying Protein Folding

3. In Vitro Folding Assays

   • Techniques to monitor protein folding in vitro (e.g., circular dichroism, fluorescence spectroscopy).
   • Refolding experiments and their protocols.
   • Kinetic and thermodynamic analysis of protein folding.

4. NMR Spectroscopy in Protein Folding

   • Using nuclear magnetic resonance (NMR) to study folding intermediates and conformational changes.
   • Protocols for preparing protein samples for NMR.

5. X-Ray Crystallography for Protein Structure

   • Crystallography methods to determine the structure of folded and misfolded proteins.
   • Procedures for crystallizing proteins and data interpretation.

6. Fluorescence Spectroscopy

   • Using fluorescence techniques to monitor folding, stability, and aggregation of proteins.
   • Applications in studying folding intermediates and misfolded aggregates.

7. Microscopy Techniques

   • Electron microscopy and other imaging techniques to study protein aggregates and amyloid fibrils.
   • Super-resolution microscopy for monitoring protein interactions.

8. Mass Spectrometry and Proteomics

   • Mass spectrometry for characterizing folding intermediates and detecting misfolded protein species.
   • Techniques for large-scale proteomics to study folding pathways in cellular contexts.

Part III: Protein Misfolding and Disease Mechanisms

9. Amyloidogenic Proteins and Aggregates

   • The formation and toxicity of amyloid fibrils.
   • Techniques to study amyloid aggregation and its implications for diseases like Alzheimer’s and Parkinson’s.

10. Protein Aggregation and Neurodegenerative Diseases

    • The role of protein aggregation in the pathogenesis of neurodegenerative diseases.
    • Protocols to measure protein aggregation and study cellular responses to misfolding.

11. Prion Proteins and Diseases

    • Molecular mechanisms of prion diseases, including the propagation of misfolded proteins.
    • Experimental models for studying prion protein misfolding.

Part IV: Therapeutic Approaches

12. Molecular Chaperones and Folding Modulators

    • Using molecular chaperones to facilitate protein folding and prevent misfolding.
    • Therapeutic strategies targeting protein folding pathways.

13. Small Molecules and Drug Discovery

    • Screening for small molecules that can stabilize protein folding or prevent aggregation.
    • Protocols for testing potential therapeutic compounds in vitro and in vivo.

14. Gene Therapy and Protein Replacement

    • Approaches to gene therapy and protein replacement in diseases caused by misfolded proteins.
    • Targeted therapies for cystic fibrosis and other folding-related disorders.

Part V: Advanced Topics and Future Directions

15. Emerging Techniques in Protein Folding Research

    • Advanced techniques such as single-molecule spectroscopy and cryo-EM for studying protein folding and misfolding.
    • New methods for monitoring real-time folding processes.

16. Model Organisms and In Vivo Studies

    • Using model organisms like yeast, C. elegans, and mice to study protein misfolding and related diseases.
    • Techniques for studying protein misfolding in living cells.

17. Computational Approaches in Protein Folding

    • Molecular dynamics simulations to model protein folding and misfolding.
    • Computational prediction of protein misfolding and aggregation.

18. Future Perspectives and Challenges

    • Open questions and challenges in the field of protein folding and misfolding.
    • The future of therapeutic strategies targeting protein misfolding.

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