Energetics of Protein Folding: why proteins fold into stable conformations?.- Introduction: Protein structure, assembly and dynamics.- Protein structural diversity: globular, multidomain and intrinsically unstructured.- The thermodynamic hypothesis of protein folding: Anfinsen s dogma.- Outlook: The amyloid state.- Protein stability: how is the folded conformation maintained?.- Physical Driving Forces for protein folding and stability.- Measuring protein stability: chemical and thermal denaturation.- Outlook: Hyperstable proteins: lessons from thermophiles and knotted proteins.- Protein Folding Kinetics and mechanisms: how do proteins fold?.- The Levinthal paradox and folding funnels.- Folding intermediates and the molten globule state.- The nucleation mechanism of protein folding.- A survey on experimental methods: time-resolved methods and the chevron plot.- Computational analysis of folding kinetics: go-model and full atomistic analysis.- Outlook: protein folding in the cell.- Protein misfolding and aggregation.- Protein aggregation, aggresomes and inclusion bodies.- Mechanisms of amyloid formation: aggregates, protofibrilis and fibrils .- Mechanisms and analysis of fibril formation .- Evolutionary adaptations to prevent aggregation (gatekeeping residues).- Outlook: protein folding and disease.
Klappentext
This snapshot volume is designed to provide a smooth entry into the field of protein folding. Presented in a concise manner, each section introduces key concepts while providing a brief overview of the relevant literature. Outlook subsections will pinpoint specific aspects related to emerging methodologies, concepts and trends.
