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.
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