Thermostable proteins : structural stability and design
Resource Information
The work Thermostable proteins : structural stability and design represents a distinct intellectual or artistic creation found in University of Missouri Libraries. This resource is a combination of several types including: Work, Language Material, Books.
The Resource
Thermostable proteins : structural stability and design
Resource Information
The work Thermostable proteins : structural stability and design represents a distinct intellectual or artistic creation found in University of Missouri Libraries. This resource is a combination of several types including: Work, Language Material, Books.
- Label
- Thermostable proteins : structural stability and design
- Title remainder
- structural stability and design
- Statement of responsibility
- [edited by] Srikanta Sen, Lennart Nilsson
- Language
- eng
- Summary
- "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"--Provided by publisher
- Cataloging source
- EBLCP
- Dewey number
-
- 572.6
- 612/.01575
- Illustrations
- illustrations
- Index
- no index present
- LC call number
- QR84.8 S76 2011
- Literary form
- non fiction
- Nature of contents
-
- dictionaries
- bibliography
- NLM call number
- QU 55.9
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- Thermostable proteins : structural stability and design, [edited by] Srikanta Sen, Lennart Nilsson
- Thermostable proteins : structural stability and design, [edited by] Srikanta Sen, Lennart Nilsson
- Thermostable proteins : structural stability and design, [edited by] Srikanta Sen, Lennart Nilsson
- Thermostable proteins : structural stability and design, [edited by] Srikanta Sen, Lennart Nilsson
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<div class="citation" vocab="http://schema.org/"><i class="fa fa-external-link-square fa-fw"></i> Data from <span resource="http://link.library.missouri.edu/resource/G9puzfmv1eY/" typeof="CreativeWork http://bibfra.me/vocab/lite/Work"><span property="name http://bibfra.me/vocab/lite/label"><a href="http://link.library.missouri.edu/resource/G9puzfmv1eY/">Thermostable proteins : structural stability and design</a></span> - <span property="potentialAction" typeOf="OrganizeAction"><span property="agent" typeof="LibrarySystem http://library.link/vocab/LibrarySystem" resource="http://link.library.missouri.edu/"><span property="name http://bibfra.me/vocab/lite/label"><a property="url" href="http://link.library.missouri.edu/">University of Missouri Libraries</a></span></span></span></span></div>