Thermostable Proteins: Structural Stability and Design provides a comprehensive, updated account of the physical basis of enhanced stability of thermophilic proteins and the design of tailor-made thermostable proteins, paving the way for their possible industrial applications. This book is devoted to understanding the survival mechanisms of "thermophilic life forms" at the molecular level with an emphasis on design strategies. The review chapters presented in Thermostable Proteins span a wide range of protein thermostability research. Basic structural, thermodynamic, and kinetic principles are explained and molecular strategies for the adaptation to high temperatures are delineated. In addition, this book covers: Computing and simulation methods in current and future thermostability research, especially in nonempirical situations How rigidity theory is used to improve the thermal adaptation of mesophiles Subtilisin-like serine proteases and their significant engineering applications The state of knowledge concerning structure-function relations and the origins of their structural stability Computational and experimental approaches for the design of proteins with increased thermal stability based on sequences or three-dimensional structures Understanding the molecular basis of how thermostable and hyperthermostable proteins gain and maintain their stability and biological function at high temperatures remains an important scientific challenge. A more detailed knowledge of protein stability not only deepens our understanding of protein structure but also helps in obtaining insights into processes that drive protein activities-folding, unfolding, and misfolding-essential to biological function.

Thermostable Proteins: Structural Stability and Design provides a comprehensive, updated account of the physical basis of enhanced stability of thermophilic proteins and the design of tailor-made thermostable proteins, paving the way for their possible industrial applications. This book is devoted to understanding the survival mechanisms of "thermophilic life forms" at the molecular level with an emphasis on design strategies.

The review chapters presented in Thermostable Proteins span a wide range of protein thermostability research. Basic structural, thermodynamic, and kinetic principles are explained and molecular strategies for the adaptation to high temperatures are delineated. In addition, this book covers:

• Computing and simulation methods in current and future thermostability research, especially in nonempirical situations
• How rigidity theory is used to improve the thermal adaptation of mesophiles
• Subtilisin-like serine proteases and their significant engineering applications
• The state of knowledge concerning structure function relations and the origins of their structural stability
• Computational and experimental approaches for the design of proteins with increased thermal stability based on sequences or three-dimensional structures

Understanding the molecular basis of how thermostable and hyperthermostable proteins gain and maintain their stability and biological function at high temperatures remains an important scientific challenge. A more detailed knowledge of protein stability not only deepens our understanding of protein structure but also helps in obtaining insights into processes that drive protein activities folding, unfolding, and misfolding essential to biological function.

This is a collection of papers presented and discussed at the first EBSA workshop held at Saltsj6baden outside stockholm in Sweden, July 6-10, 1986. The common theme of these papers is dynamics of biomolecules, and how the dynamics depends on the molecular structure and organi zation, and connects to and determines the biological function. This is a rapidly expanding field of research which combines many different aspects of molecular bio physics. Much material is new and presented for the first time. Even if the work so far has been of the kind that is usually called basic research, practical applications are clearly indicated in some articles, and are waiting around the corner in several other cases. At the workshop only one third of the time was used for the formal presentations and two thirds for discussion. To this should also be added discussions during the poster sessions. During these lively and unrecorded discussions fresh viewpoints emerged and new ideas were created. Ad mittedly, our knowledge at present is only fragmentary but when pieces of the puzzle are brought together at a workshop or in a publication of this kind more extended and sometimes unexpected contours and shapes become vi sible. It is our hope that this rapid publication of camera-ready manuscripts will transfer some of the spi rit at the workshop to the reader, and in his or her institute or laboratory initiate further discussions, bring forward more ideas and start new experimental ap roaches."