Antifreeze Proteins Volume 2: Biochemistry, Molecular Biology and Applications

Preface
Contents
Abbreviations
Chapter 1: Contents of Volume 2-Antifreeze Proteins: Biochemistry, Molecular Biology, and Application
	1.1 Part I Biochemistry and Molecular Biology of Antifreeze Proteins
	1.2 Part II Molecular Mechanisms Affected by Antifreeze Proteins
	1.3 Part III Applications of Antifreeze Proteins
Part I: The Biochemistry and Molecular Biology of Antifreeze Proteins
	Chapter 2: Characteristics of Antifreeze Proteins
		2.1 Introduction
		2.2 Structure
			2.2.1 Polar Fish
				2.2.1.1 Type I
				2.2.1.2 Type II
				2.2.1.3 Type III
				2.2.1.4 Type IV
				2.2.1.5 AFGPs
			2.2.2 Arthropods
				2.2.2.1 Insects
				2.2.2.2 Collembola
				2.2.2.3 Arachnida
				2.2.2.4 Crustacea
		2.3 Isoform Diversity
		2.4 Synthesis and Distribution
			2.4.1 Sites of Synthesis and Distribution in Polar Fish
			2.4.2 Sites of Synthesis and Distribution in Insects
		2.5 Characteristics of Ice-Binding Sites
			2.5.1 Moderately Active AF(G)Ps
			2.5.2 Hyperactive AF(G)Ps
		2.6 Conclusions
		References
	Chapter 3: Physicochemical Properties of Antifreeze Proteins
		3.1 Introduction
		3.2 Weight and Activity of Antifreeze Proteins
			3.2.1 AFPs from Fish
			3.2.2 AFPs from Arthropods
			3.2.3 Concluding the Weight and Activity Relation
		3.3 Solubility and Hydrophobicity
		3.4 Stability
			3.4.1 Thermostability
			3.4.2 pH Stability
		3.5 Conclusions
		References
	Chapter 4: Structure-Function of IBPs and Their Interactions with Ice
		4.1 Introduction
		4.2 Structural Diversity of IBPs
		4.3 Identification and Mapping of Ice-Binding Sites
		4.4 Planes Bound by AFPs
		4.5 Ice Shaping
			4.5.1 Ice Shaping Below the Hysteresis Freezing Point
			4.5.2 Ice Shaping Within the TH Gap
			4.5.3 Ice Shaping at Melting
		4.6 Size and Cooperative Effects of IBP Activity
			4.6.1 Size of AFP Molecule and Cooperativity
			4.6.2 Size of IBS
		4.7 Protein Engineering of Better IBPs
		4.8 INPs: Ice-Nucleating Proteins
		4.9 The Molecular Basis to Protein-Ice Interactions
		4.10 The Hydration Shell Theory
		4.11 The Reversible-Irreversible Binding Conflict
		4.12 The Dynamics of Binding
		4.13 Conclusions
		References
	Chapter 5: Interaction of Antifreeze Proteins with Water
		5.1 Introduction
		5.2 Structures of Antifreeze Proteins
		5.3 Structure of the Ice-Binding Site
		5.4 Solution Behavior of Antifreeze Proteins
			5.4.1 Interaction of Antifreeze Proteins with Water
				5.4.1.1 Adsorption-Inhibition Model
				5.4.1.2 Computational Studies Predict Unusual Ice-Like Hydration at the Ice-Binding Site
				5.4.1.3 Molecular Dynamics Simulations Reveal a Dual Function of the Hydration Shell and Local Melting of Ice
				5.4.1.4 X-Ray and Neutron Diffraction Reveals Ordered Hydration Waters in Crystals of Antifreeze Proteins
				5.4.1.5 Experimental Studies on the Hydration Shell Reveal Differences Between AFP Classes
		5.5 Conclusions
		References
Part II: Molecular Mechanisms Affected by Antifreeze Proteins
	Chapter 6: Thermal Hysteresis
		6.1 Introduction
		6.2 A Hysteresis Mechanism: The Kelvin Effect
			6.2.1 The Kelvin Effect: Vapor Pressure at a Curved Interface
				6.2.1.1 The Critical Radius of Curvature
			6.2.2 The Kelvin Effect at the Ice Surface
		6.3 Hysteresis Activity
			6.3.1 The Largest Intermolecular Adsorbent Gap Determines Hysteresis Activity
			6.3.2 Moderately Active and Hyperactive AF(G)Ps
				6.3.2.1 Moderate or Hyperactive: Caused by Plane Specificity and Adsorption Pattern?
		6.4 Factors That Affect the Hysteresis Activity
			6.4.1 The Factors
			6.4.2 The Solubility of the AF(G)Ps: A General Concept to Explain Variability?
				6.4.2.1 The AF(G)P/Ice Interaction Is Temperature Dependent
			6.4.3 Basic Concepts in Solubility Theory
			6.4.4 Low-Mass Additives, Solubility, and Antifreeze Potency
				6.4.4.1 The Salting-Out Constant, Ks
				6.4.4.2 Obtaining Salting-Out Constants from Measurements of Hysteresis Activity
				6.4.4.3 The Hofmeister Series and Its Linearity
				6.4.4.4 Quantitative Predictions of Protein Properties from Salt-Induced Enhancement
			6.4.5 Molecular Size, Solubility, and Antifreeze Potency
		6.5 AF(G)Ps and Ice Nucleation
			6.5.1 Biological Relevance of INAs
			6.5.2 Overall Structural Aspects of INAs
		6.6 Conclusions
		References
	Chapter 7: Inhibition of Recrystallization
		7.1 Introduction
		7.2 Ice Recrystallization Inhibition in Nature
			7.2.1 Plant Species
			7.2.2 Animals
		7.3 Ice-Binding Molecules and the Gibbs-Thomson Effect
		7.4 Fundamentals of Ice Recrystallization
			7.4.1 Ostwald Ripening
			7.4.2 Recrystallization Kinetics
			7.4.3 LSW Theory at Idealized Conditions
			7.4.4 Modifications to LSW Theory for Real Systems
			7.4.5 Recrystallization Kinetics in the Presence of Ice-Binding Molecules
			7.4.6 Summary
		7.5 Experimental Determination of Ice Recrystallization
			7.5.1 Methods
			7.5.2 Results for Different Compounds
		7.6 Conclusions
		References
	Chapter 8: Other Protective Measures of Antifreeze Proteins
		8.1 Introduction
		8.2 Stabilization of Membranes
		8.3 Antifreeze Proteins in the Context of Bacteria
		8.4 Antifreeze Proteins and Plant Pathogens
		8.5 Conclusions
		References
	Chapter 9: Measuring Antifreeze Protein Activity
		9.1 Introduction
		9.2 Quantification of AFP Activity
			9.2.1 Thermal Hysteresis
				9.2.1.1 Cryomicroscopy
				9.2.1.2 Calorimetry
		9.3 Recrystallization Inhibition
			9.3.1 Microscopy
		9.4 Detection of AFP
			9.4.1 Crystal Structure
			9.4.2 Terahertz Spectroscopy and the Hydration Shell
			9.4.3 Detection in Tissue
			9.4.4 Macroscopic and Indirect Methods
		9.5 Conclusions
		References
Part III: Applications of Antifreeze Proteins
	Chapter 10: Antifreeze Proteins in Foods
		10.1 Introduction
		10.2 Dietary Sources of Antifreeze Proteins
		10.3 Basic Functions of Antifreeze Proteins in Food
			10.3.1 Reducing the Freezing Temperature of Food
			10.3.2 Control or Prevent Recrystallization During Freeze Storage
		10.4 Application of Antifreeze Proteins to Food
			10.4.1 Ice-Cream Products
			10.4.2 Chilled and Frozen Meat and Fish
			10.4.3 Frozen Dough
			10.4.4 Fruits and Vegetables
		10.5 AFP Intake and Reliability
		10.6 Factors Affecting the Use of AFPs in Foods
		10.7 Conclusions
		References
	Chapter 11: Cell, Tissue, and Organ Preservation with Insect-Derived Antifreeze Peptides
		11.1 Introduction
		11.2 Experimental Design and Research Strategy
		11.3 Cell Preservation
		11.4 Tissue Preservation
		11.5 Organ Preservation
		11.6 Discussion
		11.7 Conclusions
		References
	Chapter 12: Antifreeze Proteins and Gas Hydrate Inhibition
		12.1 Introduction
		12.2 Thermodynamic Inhibition of Gas Hydrates
		12.3 Low-Dosage Hydrate Inhibitors
		12.4 Methods for Assessing Efficacy of Low-Dosage Hydrate Inhibitors
		12.5 Antifreeze Proteins as Gas Hydrate Inhibitors
		12.6 Conclusions
		References
	Chapter 13: Antifreeze Protein-Covered Surfaces
		13.1 Introduction
		13.2 Coating Surfaces to Prevent Icing
		13.3 Creating Anti-icing Surfaces
			13.3.1 Anti-icing Surfaces Using Polymers
			13.3.2 Anti-icing Surfaces Using Micro-/Nanostructures
		13.4 Effective Anti-icing Antifreeze Proteins from an Antarctic Diatom
		13.5 Conclusions
		References
	Chapter 14: Mutational Studies on Antifreeze Proteins
		14.1 Introduction
		14.2 Genetic Manipulation
		14.3 Tags and Fusion Proteins
			14.3.1 Purification and Yield
			14.3.2 Fluorescent Tagging
		14.4 Localising Ice-Binding Domains
		14.5 Exploring the Ice-Binding Mechanism
			14.5.1 Antifreeze Protein Type I, HPLC-6
		14.6 Improving Antifreeze Activity
			14.6.1 Polymerisation of Ice-Binding Domains
			14.6.2 Increasing the Number of Coils
			14.6.3 Fine-Tuning of the Ice-Binding Domain
		14.7 Creating Cold-Tolerant Organisms
			14.7.1 Plants
			14.7.2 Animals
			14.7.3 Unicellular Organisms
		14.8 Conclusions
		References
Part IV: Closure
	Chapter 15: Summary and Future Directions
		References