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Full Description
Although textbooks on the physics of condensed matter consider non-covalent interactions in detail, their application for analysis of protein properties is often poorly presented or omitted. On the other hand, books on biochemistry, molecular modeling or molecular simulation introduce these interactions in the context of the corresponding topic, which sometimes results in superficial explanations of their nature. This book succeeds in uniting comprehensive considerations of non-covalent interactions with the specificity of their application in protein sciences.This second edition includes new chapters on intrinsically disordered proteins, microcalorimetry of proteins, cold denaturation, thermodynamic stability and thermal adaptability of proteins. The ideal aid for students of physics or chemistry, with interests in biology and biophysics, the book can also be useful for students of biology, biochemistry, or biomedicine who want to extend their knowledge of how protein properties are described at the molecular level.
Contents
Dedication; Preface to the First Edition; Preface to the Second Edition; Introduction: Some Historical Notes; Overview of Protein Structural Elements and Basic Definitions; Non-Covalent Interactions and Structure-Function Relationships in Proteins; Van der Waals Interactions: Observation of van der Waals Interactions; Nature of van der Waals Interactions; Potential Functions for Application in Proteins; Approximation for Polyatomic Systems; Hydrogen Bonds: Nature of Hydrogen Bonds; Geometry and Strength of Hydrogen Bond; Hydrogen Bonds in Proteins; Hydrogen Bonds and Protein Stability; Hydrophobic Interactions: Nature of Hydrophobic Interactions, Pseudo Forces; Water; Hydrophobic Effect; Hydrophobic Interactions in Proteins; Electrostatic Interactions: Debye-Hückel Theory; Ion-solvent Interactions; Calculation of Electrostatic Interactions in Proteins; Ionization Equilibria in Protein: Why Does One Need to Know Ionisation Equilibria?; Basic Definitions; Factors Determining Ionisation Equilibria in Proteins; Combinatorial Problem; Cooperative Ionization; Conformational Flexibility: Location Variation of Polar Hydrogen Atoms; Examples for Ph-Dependent Hydrogen Bonding; Conformational Flexibility Involving Non-hydrogen Atoms; Protein States: Folded and Unfolded States; Misfolded Proteins; Metamorphic Proteins; Intrinsically Disordered Proteins; Modelling of Electrostatic Interactions in Unfolded Proteins: Spherical Model of Unfolded Proteins; Size of the Dielectric Sphere; Average Distance Between Charges; Ionisation Equilibria in Unfolded Proteins; Protein Stability: Definitions; Kinetic Stability; pH Dependence of Protein Stability; Temperature Dependence of Protein Stability; Thermal Stability of Proteins; Appendix A: Basic Concepts in Thermodynamics and Statistical Physics: Subject and Main Definitions of Thermodynamics; Subject and Main Definitions of Statistical Thermodynamics; Appendix B: Electric Dipoles: Definition; Electrostatic Field of a Dipole; Appendix C: Nabla-operator, Solutions of the Poisson-Boltzmann Equations: Laplace Operator; Spherical Symmetrical Form of the Laplace and Poisson-Boltzmann Equations; Solution of Laplace and Poisson-Boltzmann Equation in the Debye-Hückel Theory; Index;
