| Description |
1 online resource (x, 249 pages) : illustrations (some color) |
| Series |
Methods in molecular biology ; 752 |
|
Methods in molecular biology (Clifton, N.J.) ; v. 752
|
| Contents |
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 |
| Summary |
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 |
| Analysis |
eiwitten |
|
proteins |
|
pathologie |
|
pathology |
|
Proteins and Enzymes |
|
Eiwitten en enzymen |
| Bibliography |
Includes bibliographical references and index |
| Notes |
Print version record |
| Subject |
Protein folding.
|
|
Proteins -- Pathophysiology
|
|
Proteins -- Conformation.
|
|
Protein Folding
|
|
Protein Conformation
|
|
Proteins -- physiology
|
|
Cells -- pathology
|
|
Proteins -- Conformation
|
|
Protein folding
|
| Genre/Form |
Laboratory manuals.
|
|
Manuels de laboratoire.
|
| Form |
Electronic book
|
| Author |
Hill, Andrew F. (Andrew Francis)
|
| ISBN |
9781603272230 |
|
1603272232 |
|
