High Hydrostatic Pressure Effects in the Biosphere: from Molecules to Microbiology

作者: Filip Meersman , Karel Heremans

DOI: 10.1128/9781555815646.CH1

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摘要: This chapter aims to give an outline of the effect high hydrostatic pressure on proteins, lipids, nucleic acids, and their interactions provide a thermodynamic kinetic framework describe these effects. The effects single-component systems (e.g., protein in solution) are then related viability microorganisms under extremes pressure. A temperature increase will cause volume expansion, reduction volume. If, however, as case water, forces strong, might actually decrease volume, is observed between 0 4°C, where it reaches its maximum density ambient conditions. above-mentioned general principles become even clearer when melting (dTm/dp) solid hydrocarbons ice considered. Proteins similar prion proteins involved bovine spongiform encephalopathy Creutzfeldt-Jakob’s disease also occur, for instance, yeasts. Mapping structural features biomolecules pressure-temperature plane important research topic molecular biologist see which state physiologically relevant.

参考文章(57)
P.W. Bridgman, THE COAGULATION OF ALBUMEN BY PRESSURE Journal of Biological Chemistry. ,vol. 19, pp. 511- 512 ,(1914) , 10.1016/S0021-9258(18)88287-4
Kunihiro Seki, Masato Toyoshima, Preserving tardigrades under pressure Nature. ,vol. 395, pp. 853- 854 ,(1998) , 10.1038/27576
YUKIHISA FUJITA, YUKINAO NODA, Effect of hydration on the thermal stability of protein as measured by differential scanning calorimetry. Chymotrypsinogen A. International Journal of Peptide and Protein Research. ,vol. 18, pp. 12- 17 ,(2009) , 10.1111/J.1399-3011.1981.TB02034.X
Chieko Hashizume, Kunio Kimura, Rikimaru Hayashi, Kinetic Analysis of Yeast Inactivation by High Pressure Treatment at Low Temperatures Bioscience, Biotechnology, and Biochemistry. ,vol. 59, pp. 1455- 1458 ,(1995) , 10.1271/BBB.59.1455
Filip Meersman, L�szl� Smeller, Karel Heremans, Extending the Pressure–Temperature State Diagram of Myoglobin Helvetica Chimica Acta. ,vol. 88, pp. 546- 556 ,(2005) , 10.1002/HLCA.200590037
G. Hummer, S. Garde, A. E. Garcia, M. E. Paulaitis, L. R. Pratt, The pressure dependence of hydrophobic interactions is consistent with the observed pressure denaturation of proteins. Proceedings of the National Academy of Sciences of the United States of America. ,vol. 95, pp. 1552- 1555 ,(1998) , 10.1073/PNAS.95.4.1552
S. A. Hawley, R. M. Macleod, Pressure-temperature stability of DNA in neutral salt solutions. Biopolymers. ,vol. 13, pp. 1417- 1426 ,(1974) , 10.1002/BIP.1974.360130712
Vittorio Luzzati, Biological significance of lipid polymorphism: the cubic phases. Current Opinion in Structural Biology. ,vol. 7, pp. 661- 668 ,(1997) , 10.1016/S0959-440X(97)80075-9