Protein folding, misfolding, and disease : methods and protocols /
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 prot...
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| Format: | Book |
| Language: | English |
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New York :
Humana : Springer,
©2011
New York : Humana ; Springer, c2011 Totowa, NJ : Humana Press : Imprint: Humana Press, 2011 |
| Series: | Methods in Molecular Biology, Methods and Protocols,
752 Methods in molecular biology (Clifton, N.J.) ; v. 752 Springer Protocols (Springer-12345) Springer protocols |
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Table of Contents:
- 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
- Strategies for boosting the accumulation of correctly folded recombinant proteins expressed in Escherichia coli / Ario de Marco
- Escherichia coli cell-free system for recombinant protein synthesis on a milligram scale / Luke A. Miles ... [et al.]
- Synthesis of peptide sequences derived from fibril-forming proteins / Denis B. Scanlon and John A. Karas
- Refolding your protein with a little help from REFOLD / Jennifer Phan ... [et al.]
- Circular dichroism and its use in protein-folding studies / David T. Clarke
- Distance measurements by continuous wave EPR spectroscopy to monitor protein folding / James A. Cooke and Louise J. Brown
- Solution-state nuclear magnetic resonance spectroscopy and protein folding / Lisa D. Cabrita ... [et al.]
- Diagnostics for amyloid fibril formation : where to begin / Danny M. Hatters and Michael D.W. Griffin
- Probing protein aggregation with quartz crystal microbalances / Tuomas P.J. Knowles ... [et al.]
- Dried and hydrated x-ray scattering analysis of amyloid fibrils / Sally L. Gras and Adam M. Squires
- Solid-state NMR of amyloid membrane interactions / John D. Gehman and Frances Separovic
- Sedimentation velocity analysis of amyloid fibrils / Chi Le Lan Pham, Yee-Foong Mok, and Geoffrey J. Howlett
- Transmission electron microscopy of amyloid fibrils / Sally L. Gras, Lynne J. Waddington, and Kenneth N. Goldie
- Surface plasmon resonance spectroscopy : a new lead in studying the membrane binding of amyloidogenic transthyretin / Xu Hou, David H. Small, and Marie-Isabel Aguilar
- Elucidating the role of metals in Alzheimer's disease through the use of surface-enhanced laser desorption/ionisation time-of-flight mass spectrometry / Andrew D. Watt, Keyla A. Perez, and Lin Wai Hung
- Strategies for boosting the accumulation of correctly folded recombinant proteins expressed in Escherichia coli / Ario de Marco
- Escherichia coli cell-free system for recombinant protein synthesis on a milligram scale / Luke A. Miles [and others]
- Synthesis of peptide sequences derived from fibril-forming proteins / Denis B. Scanlon and John A. Karas
- Refolding your protein with a little help from REFOLD / Jennifer Phan [and others]
- Circular dichroism and its use in protein-folding studies / David T. Clarke
- Distance measurements by continuous wave EPR spectroscopy to monitor protein folding / James A. Cooke and Louise J. Brown
- Solution-state nuclear magnetic resonance spectroscopy and protein folding / Lisa D. Cabrita [and others]
- Diagnostics for amyloid fibril formation : where to begin / Danny M. Hatters and Michael D.W. Griffin
- Probing protein aggregation with quartz crystal microbalances / Tuomas P.J. Knowles [and others]
- Dried and hydrated x-ray scattering analysis of amyloid fibrils / Sally L. Gras and Adam M. Squires
- Solid-state NMR of amyloid membrane interactions / John D. Gehman and Frances Separovic
- Sedimentation velocity analysis of amyloid fibrils / Chi Le Lan Pham, Yee-Foong Mok, and Geoffrey J. Howlett
- Transmission electron microscopy of amyloid fibrils / Sally L. Gras, Lynne J. Waddington, and Kenneth N. Goldie
- Surface plasmon resonance spectroscopy : a new lead in studying the membrane binding of amyloidogenic transthyretin / Xu Hou, David H. Small, and Marie-Isabel Aguilar
- Elucidating the role of metals in Alzheimer's disease through the use of surface-enhanced laser desorption/ionisation time-of-flight mass spectrometry / Andrew D. Watt, Keyla A. Perez, and Lin Wai Hung