Protein Folding: An Introduction

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