Misbehaving Proteins: Protein (Mis)Folding, Aggregation, and Stability by Regina MurphyMisbehaving Proteins: Protein (Mis)Folding, Aggregation, and Stability by Regina Murphy

Misbehaving Proteins: Protein (Mis)Folding, Aggregation, and Stability

EditorRegina Murphy, Amos Tsai

Hardcover | May 24, 2006

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This text provides an up-to-date collection of theoretical and experimental studies into protein folding, misfolding, aggregation, and stability. Additionally, issues faced during the development of protein products are illustrated. It contains an introductory chapter for readers new to the protein folding field. The book provides a thorough and clear discussion of computational approaches to understanding and modeling protein aggregation.
Title:Misbehaving Proteins: Protein (Mis)Folding, Aggregation, and StabilityFormat:HardcoverDimensions:362 pages, 9.25 × 6.1 × 0 inPublished:May 24, 2006Publisher:Springer New YorkLanguage:English

The following ISBNs are associated with this title:

ISBN - 10:0387305084

ISBN - 13:9780387305080

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Table of Contents

Protein Folding, Misfolding, Stability and Aggregation.- Non-native Protein Aggregration.- Simulations of Protein Aggregation.- Elucidating Structure, Stability, and Conformational Distributions during Protein Aggregation with Hydrogen Exchanage and Mass Spectrometry.- Application of Spectroscopic and Calorimetric Techniques in Protein Formulation Development.- Small Angle Neutron Scattering as a Probe for Protein Aggregation at Many Length Scales.- Laser Light Scattering as an Indispensible Tool for Probing Protein Aggregation.- X-Ray Diffraction for Characterizing Structure in Protein Aggregates.- Glass Dynamics and the Preservation of Proteins.- Folding and Misfolding as a Function of Polypeptide Chain Elongation.- Determinants of Protein Folding and Aggregation in P22 Tailspike Protein.- Factors Affecting the Fibrillation of a-Synuclein, a Natively-Unfolded Protein.- Molten Globule-Lipid Bilayer Interactions and Their Implications for Protein Transport and Aggregation.- Self-Association of Therapeutic Proteins.- Mutational Approaches to Improve Physical Stability of Protein Therapeutics Susceptible to Aggregation.