Srikanta Sen – författare

This book covers the basic structural, thermodynamic and kinetic principles are covered and molecular strategies for the adaptation to high temperatures revealed by structure analysis are delineated. The roles of fluctuations, hydration and internal packing are thoroughly dicussed. Enzymes with a particular industrial importance, the subtilisin-like serine proteases, have been extensively studied by protein engineering. One extensive chapter is devoted to the present state of knowledge concerning structure-function relations and the origin of the their structural stability. Last but not least, computational and experimental approaches for the design of proteins with increased thermal stability based on sequences or 3D structures are present

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 situationsHow rigidity theory is used to improve the thermal adaptation of mesophilesSubtilisin-like serine proteases and their significant engineering applicationsThe state of knowledge concerning structure–function relations and the origins of their structural stabilityComputational and experimental approaches for the design of proteins with increased thermal stability based on sequences or three-dimensional structuresUnderstanding 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 situationsHow rigidity theory is used to improve the thermal adaptation of mesophilesSubtilisin-like serine proteases and their significant engineering applicationsThe state of knowledge concerning structure–function relations and the origins of their structural stabilityComputational and experimental approaches for the design of proteins with increased thermal stability based on sequences or three-dimensional structuresUnderstanding 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.