AI Article Synopsis
- High pressure is an effective method for gently pasteurizing food, preserving vitamins and taste while minimizing undesired changes.
- High pressure also aids in studying protein structure, revealing conformations that are difficult to achieve with temperature changes alone.
- The review discusses how high pressure affects the structures of different prion isoforms, highlighting their unique behaviors and potential implications for understanding infectious TSE material.
Article Abstract
Application of high pressure can be used for gentle pasteurizing of food, minimizing undesirable alterations such as vitamin losses and changes in taste and color. In addition, pressure has become a useful tool for investigating structural changes in proteins. Treatments of proteins with high pressure can reveal conformations that are not obtainable by other physical variables like temperature, since pressure favors structural transitions accompanied with smaller volumes. Here, we discuss both the potential use of high pressure to inactivate infectious TSE material and the application of this thermodynamic parameter for the investigation of prion folding. This review summarizes our findings on the effects of pressure on the structure of native infectious scrapie prions in hamster brain homogenates and on the structure of infectious prion rods isolated from diseased hamsters brains. Native prions were found to be pressure sensitive, whereas isolated prions revealed an extreme pressure-resistant structure. The discussion will be focused on the different pressure behavior of these prion isoforms, which points out differences in the protein structure that have not been taken into consideration before.
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| http://dx.doi.org/10.1016/j.bbapap.2005.12.018 | DOI Listing |
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