Journal ArticleDOI
Thermophilic adaptation of proteins.
Reinhard Sterner,Wolfgang Liebl +1 more
TLDR
Not all proteins from hyperthermophiles are thermostable enough to retain their structures and functions at the high physiological temperatures, and it will be shown how this shortcoming can be surpassed by extrinsic factors such as large molecular chaperones and small compatible solutes.Abstract:
Hyperthermophilic organisms optimally grow close to the boiling point of water. As a consequence, their macromolecules must be much more thermostable than those from mesophilic species. Here, proteins from hyperthermophiles and mesophiles are compared with respect to their thermodynamic and kinetic stabilities. The known differences in amino acid sequences and three-dimensional structures between intrinsically thermostable and thermolabile proteins will be summarized, and the crucial role of electrostatic interactions for protein stability at high temperatures will be highlighted. Successful attempts to increase the thermostability of proteins, which were either based on rational design or on directed evolution, are presented. The relationship between high thermo-stability of enzymes from hyperthermophiles and their low catalytic activity at room temperature is discussed. Not all proteins from hyperthermophiles are thermostable enough to retain their structures and functions at the high physiological temperatures. It will be shown how this shortcoming can be surpassed by extrinsic factors such as large molecular chaperones and small compatible solutes. Finally, the potential of thermostable enzymes for biotechnology is discussed.read more
Citations
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Journal ArticleDOI
An integrated view of protein evolution
TL;DR: The status of a much-needed coherent view that integrates studies on protein evolution with biochemistry and functional and structural genomics is discussed.
Journal ArticleDOI
Extremophiles as a source for novel enzymes.
TL;DR: Novel developments in the cultivation and production of extremophiles, but also developments related to the cloning and expression of their genes in heterologous hosts, will increase the number of enzyme-driven transformations in chemical, food, pharmaceutical and other industrial applications.
Journal ArticleDOI
Iterative saturation mutagenesis on the basis of B factors as a strategy for increasing protein thermostability
Journal ArticleDOI
How do thermophilic proteins deal with heat
Sandeep Kumar,Ruth Nussinov +1 more
TL;DR: A large number of sequence and structural factors are thought to contribute toward higher intrinsic thermal stability of proteins from hyperthermophilic and thermophilic organisms, the most consistent are surface loop deletion, increased occurrence of hydrophobic residues with branched side chains and an increased proportion of charged residues at the expense of uncharged polar residues.
Journal ArticleDOI
Rational engineering of enzyme stability.
Vincent G. H. Eijsink,Alexandra Bjørk,Sigrid Gåseidnes,Reidun Sirevåg,Bjørnar Synstad,Bertus van den Burg,Gert Vriend +6 more
TL;DR: Recent developments in the field include increasing awareness of the importance of the protein surface for stability, as well as the notion that normally a very limited number of mutations can yield a large increase in stability.
References
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Bernd Bukau,Arthur L. Horwich +1 more
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