Misbehaving Proteins : Protein (Mis)Folding, Aggregation, and Stability / by Regina M. Murphy, Amos M. Tsai.

Springer eBooks

Protein Folding, Misfolding, Stability, and Aggregation -- Mathematical Models and Computational Methods -- Nonnative Protein Aggregation -- Simulations of Protein Aggregation -- Experimental Methods -- Elucidating Structure, Stability, and Conformational Distributions during Protein Aggregation with Hydrogen Exchange 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 Indispensable Tool for Probing Protein Aggregation -- X-ray Diffraction for Characterizing Structure in Protein Aggregates -- Glass Dynamics and the Preservation of Proteins -- Fundamental Studies in Model Systems -- 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 ?-Synuclein, a Natively Unfolded Protein -- Molten Globule-Lipid Bilayer Interactions and Their Implications for Protein Transport and Aggregation -- Protein Product Development -- Self-Association of Therapeutic Proteins -- Mutational Approach to Improve Physical Stability of Protein Therapeutics Susceptible to Aggregation.

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. The first section of contributed papers covers advances in computational efforts to examine protein aggregation. In the middle section, several leading researchers describe fundamental experimental efforts to explore the relationships between protein sequence, folded structure, aggregation kinetics, and aggregate morphology. In the final part of the book, contributors discuss the practical issues arising during product development efforts because of the propensity for engineered proteins to misfold and aggregate.

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