Misbehaving Proteins

Protein (Mis)Folding, Aggregation, and Stability

Häftad, Engelska, 2010

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Beskrivning

Misbehaving Proteins: Protein (Mis)folding, Aggregation, and Stability differs from theseotherrecenteffortsinitsemphasisonfundamentalcomputationalandexperimental studies and in its linkage of disparate consequences of protein misfolding (e.g., from clinical manifestations to manufacturing headaches) to their common causes.

Produktinformation

Utgivningsdatum:2010-11-29
Mått:155 x 235 x 20 mm
Vikt:552 g
Format:Häftad
Språk:Engelska
Antal sidor:354
Förlag:Springer-Verlag New York Inc.
ISBN:9781441921420

Utforska kategorier

Biokemi inom Naturvetenskap och teknik
Analytisk kemi inom Naturvetenskap och teknik
Biokemisk teknik inom Naturvetenskap och teknik

Innehållsförteckning

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.