Protein Folding, Misfolding, and Disease [electronic resource] : Methods and Protocols / edited by Andrew F. Hill, Kevin J. Barnham, Stephen P. Bottomley, Roberto Cappai.

Totowa, NJ : Humana Press : Imprint: Humana Press, 2011.
Methods in Molecular Biology, Methods and Protocols, 1064-3745 ; 752
Springer Protocols (Springer-12345)
Methods in Molecular Biology, Methods and Protocols, 1064-3745 ; 752
1 online resource (X, 230 pages) : 50 illustrations.
Life sciences.
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Life Sciences. (search)
Protein Science. (search)
Pathology. (search)
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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.
Strategies for Boosting the Accumulation of Correctly Folded Recombinant Proteins Expressed in Escherichia coli
An Escherichia coli Cell-Free System for Recombinant Protein Synthesis on a Milligram Scale
Synthesis of Peptide Sequences Derived from Fibril-Forming Proteins
Refolding Your Protein with a Little Help from REFOLD
Circular Dichroism and Its Use in Protein Folding Studies
Distance Measurements by Continuous Wave EPR Spectroscopy to Monitor Protein Folding
Solution-State Nuclear Magnetic Resonance Spectroscopy and Protein Folding
Diagnostics for Amyloid Fibril Formation: Where to Begin
Probing Protein Aggregation with Quartz Crystal Microbalances
Dried and Hydrated X-Ray Scattering Analysis of Amyloid Fibrils
Solid-State NMR of Amyloid Membrane Interactions
Sedimentation Velocity Analysis of Amyloid Fibrils
Transmission Electron Microscopy of Amyloid Fibrils
Surface Plasmon Resonance Spectroscopy: A New Lead in Studying the Membrane Binding of Amyloidogenic Transthyretin
Elucidating the Role of Metals in Alzheimer's Disease through the Use of Surface Enhanced Laser Desorption / Ionisation Time-of-Flight Mass Spectrometry.
Hill, A. F. (Andrew F.), editor.
Barnham, Kevin J. editor.
Bottomley, Stephen P. editor.
Cappai, Roberto. editor.
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10.1007/978-1-60327-223-0 doi
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