PRESSURE AND PROTEIN DENATURATION
نویسندگان
چکیده
منابع مشابه
Pressure and protein denaturation.
Kinetic analyses have indicated that moderate hydrostatic pressures, up to some 700 atmospheres, oppose reversible and irreversible denaturations of certain enzyme systems, apparent at temperatures above the normal optimum of the enzyme reaction, as well as at lower temperatures in the presence of denaturants such as alcohol (14). Qualitative observations have shown that such pressures also ret...
متن کاملHysteresis in Pressure-Driven DNA Denaturation
In the past, a great deal of attention has been drawn to thermal driven denaturation processes. In recent years, however, the discovery of stress-induced denaturation, observed at the one-molecule level, has revealed new insights into the complex phenomena involved in the thermo-mechanics of DNA function. Understanding the effect of local pressure variations in DNA stability is thus an appealin...
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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...
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The results of a thermodynamic calculation of the excess heat capacity that is based on experimental observations and that incorporates the effects of ligand binding on the two-state, thermal denaturation of a protein are presented. For a protein with a single-binding site on the native species and at subsaturating concentrations of ligand, bimodal or unimodal thermograms were computed merely b...
متن کاملHow water contributes to pressure and cold denaturation of proteins
The mechanisms of coldand pressure-denaturation of proteins are matter of debate and are commonly understood as due to water-mediated interactions. Here we study several cases of proteins, with or without a unique native state, with or without hydrophilic residues, by means of a coarse-grain protein model in explicit solvent. We show, using Monte Carlo simulations, that taking into account how ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1946
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(17)41299-3