Cold Denaturation of Encapsulated Ubiquitin
نویسندگان
چکیده
منابع مشابه
[Cold denaturation of staphylococcal nuclease].
It has been shown that the structure of staphylococcal nuclease breaks down reversibly both at a temperature increase above 20 degrees C and at its decrease. Both the heat and cold denaturations of protein are well approximated by a transition between two states differing in heat capacity, which means that the whole protein molecule represents a unique cooperative system with a well developed h...
متن کاملMicroscopic mechanism for cold denaturation.
We elucidate the mechanism of cold denaturation through constant-pressure simulations for a model of hydrophobic molecules in an explicit solvent. We find that the temperature dependence of the hydrophobic effect induces, facilitates, and is the driving force for cold denaturation. The physical mechanism underlying this phenomenon is identified as the destabilization of hydrophobic contact in f...
متن کاملHigh-pressure NMR reveals close similarity between cold and alcohol protein denaturation in ubiquitin.
Proteins denature not only at high, but also at low temperature as well as high pressure. These denatured states are not easily accessible for experiment, because usually heat denaturation causes aggregation, whereas cold or pressure denaturation occurs at temperatures well below the freezing point of water or pressures above 5 kbar, respectively. Here we have obtained atomic details of the pre...
متن کاملFolding kinetics of proteins and cold denaturation.
Folding kinetics of a lattice model of protein is studied. It uses the random energy model for the intrachain couplings and a temperature dependent free energy of solvation derived from a realistic hydration model of apolar solutes. The folding times are computed using Monte Carlo simulations in the region of the phase diagram where the chain occurs in the native structure. These folding times ...
متن کاملTheory of cold denaturation of proteins
A new approach to the problem of cold denaturation is presented. It is based on solvent-induced effects operating on hydrophilic groups along the protein. These effects are stronger than the corresponding hydrophobic effects, and they operate on the hydrophilic groups which are plentiful than hydrophobic groups. It is shown that both heat and cold denaturation can be explained by these hydrophi...
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ژورنال
عنوان ژورنال: Journal of the American Chemical Society
سال: 2006
ISSN: 0002-7863,1520-5126
DOI: 10.1021/ja0628654