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Amyloid, prions, and other protein aggregates. Part C /

The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part C (volume 413) on Amyloid, Prions and other Pr...

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Detalles Bibliográficos
Clasificación:Libro Electrónico
Otros Autores: Kheterpal, Indu, Wetzel, Ronald
Formato: Electrónico eBook
Idioma:Inglés
Publicado: Amsterdam ; Boston : Elsevier/Academic, �2006.
Colección:Methods in enzymology ; v. 413.
Temas:
Acceso en línea:Texto completo
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MARC

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245 0 0 |a Amyloid, prions, and other protein aggregates.  |n Part C /  |c edited by Indu Kheterpal, Ronald Wetzel. 
260 |a Amsterdam ;  |a Boston :  |b Elsevier/Academic,  |c �2006. 
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490 1 |a Methods in enzymology ;  |v v. 413 
504 |a Includes bibliographical references and indexes. 
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520 |a The ability of polypeptides to form alternatively folded, polymeric structures such as amyloids and related aggregates is being increasingly recognized as a major new frontier in protein research. This new volume of Methods in Enzymology along with Part C (volume 413) on Amyloid, Prions and other Protein Aggregates continue in the tradition of the first volume (309) in containing detailed protocols and methodological insights, provided by leaders in the field, into the latest methods for investigating the structures, mechanisms of formation, and biological activities of this important class of protein assemblies. * Presents detailed protocols * Includes troubleshooting tips * Provides coverage on structural biology, computational methods, and biology. 
505 0 |a Cover; Copyright page; Table of Contents; Contributors to Volume 413; Preface; Volume in series; Chapter 1: Purification of Polyglutamine Proteins; Abstract; Introduction; Ataxin-3 Constructs Used; Manipulation of the Polyglutamine Tract Length Using Cassette Mutagenesis; Expression and Purification of Ataxin-3; Quality Control and Analysis of Purified Ataxin-3; Conclusion; References; Chapter 2: Preparation of Amyloid beta-Protein for Structural and Functional Studies; Abstract; Background; Theoretical and Practical Aspects of Amyloid Protein Preparation. 
505 8 |a Preparing Abeta for Biophysical and Biological StudyAcknowledgments; References; Chapter 3: Kinetics and Thermodynamics of Amyloid Assembly Using a High-Performance Liquid Chromatography-Based Sedimentation Assay; Abstract; Introduction; Disaggregation of Peptides; Preparation of Stocks of Aggregate Seeds; An HPLC Sedimentation Assay for Amyloid Transformations; Titration of Fibril Growing Ends; Elongation Kinetics; Nucleation Kinetics Analysis; Thermodynamics of Amyloid Fibril Elongation; Concluding Remarks; Acknowledgment; References. 
505 8 |a Chapter 4: Protein Aggregation Starting From The Native Globular StateAbstract; Introduction; Basic Features of Our Approach; Aggregation Mechanism of HypF-N; Aggregation Mechanism of Sso AcP; Conclusions; References; Chapter 5: Direct Observation of Amyloid Growth Monitored by Total Internal Reflection Fluorescence Microscopy; Abstract; Introduction; TIRFM; Direct Observation of Amyloid beta (1-40) Fibrils; Conclusion; Acknowledgments; References; Chapter 6: Characterization of Amyloid Structures at the Molecular Level by Solid State Nuclear Magnetic Resonance Spectroscopy; Abstract. 
505 8 |a IntroductionDetermination of Secondary Structure; Determination of Tertiary Structure; Determination of Quaternary Structure; Construction of Molecular Models Based on Solid State NMR Data; Sample Preparation for Solid State NMR; Acknowledgments; References; Chapter 7: Spin Labeling Analysis of Amyloids and Other Protein Aggregates; Abstract; Introduction; Application to Amyloids and Other Protein Aggregates; Outlook; Acknowledgments; References; Chapter 8: Hydrogen/Deuterium Exchange Mass Spectrometry Analysis of Protein Aggregates; Abstract; Introduction. 
505 8 |a Technological Considerations in H/D Exchange-MSH/D Exchange into Abeta(1-40) Fibrils; Achieving Higher Spatial Resolution by On-Line H/D Exchange-MS with Proteolysis; Proteolysis of Abeta(1-40) Amyloid Fibrils; Conclusions; Acknowledgments; References; Chapter 9: Hydrogen-Deuterium Exchange Analyzed by Matrix-Assisted Laser Desorption-Ionization Mass Spectrometry and the HET-s Prion Model; Abstract; Introduction; Materials and Methods; Results; Future Perspective: Improving the Resolution of HXMS Experiments; Conclusion; Acknowledgments; References. 
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653 1 0 |a Proteins and Enzymes 
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700 1 |a Kheterpal, Indu. 
700 1 |a Wetzel, Ronald. 
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