Protein Stabilization by Osmolytes from Hyperthermophiles
نویسندگان
چکیده
منابع مشابه
Protein stabilization by naturally occurring osmolytes.
Natural selection is believed to be an unforgiving and relentless force in the evolution of life on earth. An organism that cannot adapt to a changing environment or an environment hostile to cell functions is at risk as a species. So it is important to understand the mechanisms used by plants, animals, and microorganisms in adapting to environments in the biosphere that would ordinarily denatu...
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We determined the added enthalpic and entropic contributions of protective osmolytes to the folding of a model peptide into its native beta-hairpin state. In contrast to entropically driven steric "crowding", this study shows that sugars and polyols can act as protective osmolytes by primarily diminishing the unfavourable enthalpic contribution to folding.
متن کاملProtein thermal stabilization in aqueous solutions of osmolytes.
Proteins' thermal stabilization is a significant problem in various biomedical, biotechnological, and technological applications. We investigated thermal stability of hen egg white lysozyme in aqueous solutions of the following stabilizing osmolytes: Glycine (GLY), N-methylglycine (NMG), N,N-dimethylglycine (DMG), N,N,N-trimethylglycine (TMG), and trimethyl-N-oxide (TMAO). Results of CD-UV spec...
متن کاملAssaying Enzymes from Hyperthermophiles
The determination of kinetic and thermodynamic data from hyperthermophilic enzymes at physiological temperature (i. e. ‡ 80 C) raises a number of technical and fundamental problems. Based on studies of purified enzymes from the model organism Pyrococcus furiosus several of these problems are identified and explored here. It is proposed that kinetic and thermodynamic data on hyperthermophilic en...
متن کاملData on the role of accessible surface area on osmolytes-induced protein stabilization
This paper describes data related to the research article "Testing the dependence of stabilizing effect of osmolytes on the fractional increase in the accessible surface area on thermal and chemical denaturations of proteins" [1]. Heat- and guanidinium chloride (GdmCl)-induced denaturation of three disulfide free proteins (bovine cytochrome c (b-cyt-c), myoglobin (Mb) and barstar) in the presen...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2004
ISSN: 0021-9258
DOI: 10.1074/jbc.m408806200