Biochemistry and Function of Antifreeze Proteins

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Editor: Steffen P. Graether

Antifreeze proteins, also known as thermal hysteresis proteins, ice binding proteins and ice structuring proteins, prevent the growth of ice crystals in several cold blooded organisms. First discovered in fish, they have also been found in insects, plants, fungi and bacteria. Antifreeze proteins cause the non-colligative depression of the freezing point of water, a property which has been exploited in the practical applications of antifreeze proteins such as improving the texture of ice cream, and could be used to extend the crop growing season or allow fish to thrive in cold waters. This book provides clear information on what is known about antifreeze proteins today and how to study them.

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Description

Preface

Chapter 1. Robert E. Feeney: Courage and Vision
(Yin Yeh, University of California, Davis, CA)

Chapter 2. Measuring Antifreeze Activity
(Hans Ramløv, Roskilde University, Denmark)

Chapter 3. Gene Regulation of Antifreeze Proteins
(Michael G. Tyshenko, University of Ottawa, Canada)

Chapter 4. Ice Nucleation and Antifreeze Proteins in Animals
(Karl Erik Zachariassen, Norwegian University of Science and Technology; John G. Duman, University of Notre Dame; Erlend Kristiansen, Norwegian University of Science and Technology; Sindre Pedersen, Norwegian University of Science and Technology; Natalia Li Russian Academy of Science, Yakutsk)

Chapter 5. Structure and Functional Dynamics of Antifreeze Glycoproteins
(V. V. Krishnan and Yin Yeh, University of California, Davis, CA)

Chapter 6. Structure and Function of Antifreeze Proteins
(Steffen P. Graether, University of Guelph, Guelph, ON)

Chapter 7. Antifreeze Proteins: A Computational Perspective from the Past 10 Years
(Jeffry D. Madura, Duquesne University Pittsburgh, PA; Andrzej Wierzbicki, University of South Alabama, Mobile, AL; Jun Cui, Duquesne University Pittsburgh, PA; Keith Battle, Duquesne University Pittsburgh, PA and University of South Alabama, Mobile, AL)

Index

Additional information

Binding

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