BookClaudio M. Gomes, Patricía F.N. Faísca.
Summary: 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.
Contents:
Intro; Preface; Contents; About the Authors; 1 Protein Folding: An Introduction; 1 Protein Structure-How Is Structure Maintained?; 1.1 The Dawn of Protein Structural Biology; 1.2 The Universe of Protein Structures; 1.3 Physical Interactions Stabilising Proteins; 1.4 Protein Dynamics and Solvation; 2 Protein Folding-Why Is Structure Acquired?; 2.1 The Anfinsen Experiments; 2.2 The Thermodynamic Hypothesis; 2.3 Driving Forces for Protein Folding-Hydrophobic Effect and the Thermodynamics of Protein Folding; 3 Folding Kinetics and Mechanisms: How Is Structure Acquired? 3.1 Two-State Cooperativity in Protein Folding3.2 The Levinthal Paradox and the Timescale of Protein Folding; 3.3 Mechanisms of Protein Folding; 3.4 The Nucleation Condensation Mechanism of Protein Folding; 3.5 Phi-value Analysis and the Structure of the Folding Transition State; 3.6 The Energy Landscape and Folding Funnels; 3.7 The Importance of Native Geometry as a Determinant of Folding Rates; 3.8 The Folding Mechanism of Knotted Proteins; 4 Protein Misfolding: Why Proteins Misbehave?; 4.1 Protein Folding In Vivo; 4.2 Protein Misfolding and Aggregation; 4.3 Protein Misfolding Diseases 4.4 The Amyloid State4.5 Mechanism and Kinetics of Protein Aggregation; 4.6 Aggregation Propensity; 5 Methods for Protein Folding; 5.1 Biophysical Spectroscopies; 5.2 Computational Methods; References