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    Thermostable Proteins: Structural Stability and Design (repost)

    Posted By: libr
    Thermostable Proteins: Structural Stability and Design (repost)

    Thermostable Proteins: Structural Stability and Design by Srikanta Sen and Lennart Nilsson
    English | 2011 | ISBN-10: 1439839131 | 187 pages | PDF | 12,7 MB

    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.