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Protein folding, misfolding, and disease : methods and protocols / edited by Andrew F. Hill ... [et al]. — New York : Huaman Press, c2011. – (58.17/M592/v.752) |
Contents
CONTENTS
Preface
Contributors
1 Strategies for Boosting the Accumulation of Correctly Folded Recombinant Proteins Expressed in Escherichia coli
2 An Escherichia coli Cell-Free System for Recombinant Protein Synthesis on a Milligram Scale
3 Synthesis of Peptide Sequences Derived from Fibril-Forming Proteins
4 Refolding Your Protein with a Little Help from REFOLD
5 Circular Dichroism and Its Use in Protein-Folding Studies
6 Distance Measurements by Continuous Wave EPR Spectroscopy to Monitor Protein Folding 73
7 Solution-State Nuclear Magnetic Resonance Spectroscopy and Protein Folding 97
8 Diagnostics for Amyloid Fibril Formation: Where to Begin? 121
9 Probing Protein Aggregation with Quartz Crystal Microbalances 137
10 Dried and Hydrated X-Ray Scattering Analysis of Amyloid Fibrils 147
11 Solid-State NMR of Amyloid Membrane Interactions
12 Sedimentation Velocity Analysis of Amyloid Fibrils
13 Transmission Electron Microscopy of Amyloid Fibrils
14 Surface Plasmon Resonance Spectroscopy: A New Lead in Studying the Membrane Binding of Amyloidogenic Transthyretin
15 Elucidating the Role of Metals in Alzheimer's Disease Through the Use of Surface-Enhanced Laser Desorption/Ionisation Time-of-Flight Mass Spectrometry
Index