Thermodynamic stability and folding of proteins from hyperthermophilic organisms
نویسندگان
چکیده
منابع مشابه
Osmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization
It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
متن کاملOsmolyte-Induced Folding and Stability of Proteins: Concepts and Characterization
It is well-known that the typical protein’s three-dimensional structure is relatively unstable in harsh conditions. A practical approach to maintain the folded state and thus improve the stability and activity of proteins in unusual circumstances is to directly apply stabilizing substances such as osmolytes to the protein-containing solutions. Osmolytes as natural occurring organic molecules ty...
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The apical domain of GroEL (residues 191 to 376) and its C-terminally truncated fragment GroEL(191-345) are expressed with high yield in Escherichia coli to give functional monomeric minichaperones. Owing to the reversible folding behaviour of the minichaperones we can analyse the folding of the polypeptide binding domain of the multidomain GroEL protein, the folding of which is known to be irr...
متن کاملReverse gyrase and genome stability in hyperthermophilic organisms.
Reverse gyrase is a DNA topoisomerase that is peculiar in many aspects: it has the unique ability to introduce positive supercoils into DNA molecules; it comprises a type IA topoisomerase fused to a helicase-like domain; although it is a type IA topoisomerase, its reaction is ATP-dependent; and it is the only hyperthermophile-specific protein. All these features have made reverse gyrase the sub...
متن کاملThermodynamic stability of folded proteins against mutations
By balancing the average energy gap with its typical change due to mutations for protein-like heteropolymers with M residues, we show that native states are unstable to mutations on a scale M ∼ (λ/σμ) 1/ζs , where λ is the dispersion in the interaction free energies and σμ their typical change. Theoretical bounds and numerical estimates (based on complete enumeration on four lattices) of the in...
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ژورنال
عنوان ژورنال: FEBS Journal
سال: 2007
ISSN: 1742-464X
DOI: 10.1111/j.1742-4658.2007.05955.x