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High-Pressure NMR Experiments for Detecting Protein Low-Lying Conformational States
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Dynamic structural changes in microbial membranes in response to high hydrostatic pressure analyzed using

Fumiyoshi Abe1

  • 1Department of Chemistry and Biological Science, College of Science and Engineering, Aoyama Gakuin University, Sagamihara, Japan; Institute of Biogeosciences, Japan Agency for Marine-Earth Science and Technology (JAMSTEC), Yokosuka, Japan.

Biophysical Chemistry
|June 25, 2013
PubMed
Summary

Deep-sea organisms use specialized cell membranes to adapt to high hydrostatic pressure. Eicosapentaenoic acid plays a key role in maintaining membrane structural integrity under extreme pressure conditions.

Keywords:
1,6-diphenyl-1,3,5-hexatriene1-[4-(trimethylamino)pheny]-6-phenyl-1,3,5-hexatrieneD(w)DHADOPCDPHDPPCDSPCDeep-sea piezophileEPAHP-TRFAMHigh-pressure time-resolved fluorescence anisotropy measurement (HP-TRFAM)Membrane fluidityPOPCPUFASSAPCSDPCSOPCTCSPCTMA-DPHdioleyl-phosphatidylcholinedipalmitoyl-phosphatidylcholinedistearoyl-phosphatidylcholinedocosahexaenoic acid (C22:6)eicosapentaenoic acid (C20:5)fluorescence anisotropyhigh-pressure time-resolved fluorescence anisotropy measurementorder parameterpalmitoyl-oleoyl-phosphatidylcholinepolyunsaturated fatty acidsrrotational diffusion coefficientstearoyl-arachidonoyl-phosphatidylcholinestearoyl-docosahexanoylphosphatidylcholinestearoyl-oleyl-phosphatidylcholinetime-correlated single-photon counting

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