Protein Condensation Kinetic Pathways to Crystallization and Disease

About this book

The quest to understand the condensation of proteins from solutions is a rapidly evolving field. The purpose of Protein Condensation is to bring to an interdisciplinary audience the state-of-the-art in current research. The first part of Protein Condensation deals with issues related to the production of high quality protein crystals from solution. Since protein function is determined by structure, high quality protein crystals must be grown in order to determine their structure by X-ray crystallography. Protein Condensation also discusses diseases that occur due to undesired protein condensation, an increasingly important subject. Examples include sickle cell anemia, cataracts and Alzheimer's disease. Current experimental and theoretical work on these diseases is discussed, which seeks understanding at a fundamental, molecular level, to prevent the undesired condensation from occurring.

Contents

Preface

1. Introduction
2. Globular protein structure
3. Experimental methods
4. Thermodynamics and statistical mechanics
5. Protein-protein interactions
6. Theoretical studies of equilibrium
7. Nucleation theory
8. Experimental studies of nucleation
9. Lysozyme
10. Some other globular proteins
11. Membrane proteins
12. Crystallins and cataracts
13. Sickle hemoglobin and sickle cell anemia
14. Alzheimer's disease

Index

Customer Reviews

Biography

J. D. Gunton is Joseph A. Waldschmitt Professor of Physics at Lehigh University in Pennsylvania. He is the author of approximately 200 articles in refereed journals on equilibrium and nonequilibrium phase transitions. He is a Rhodes Scholar and a Danforth Fellow, and a Fellow of the American Physical Society.

A. Shiryayev is a doctoral candidate at Lehigh University. He has already published several refereed articles that deal with the condensation of globular proteins.

D. L. Pagan received is PhD degree from Lehigh University in 2005. He has authored several refereed articles on the condensation of globular proteins.