• Title of article

    NMR and parity violation: low-temperature dependence in 1H CRAMPS and 13C CP/MAS ssNMR spectra of alanine enantiomer Original Research Article

  • Author/Authors

    Wenqing Wang، نويسنده , , Wei Min، نويسنده , , Zhi Liang، نويسنده , , Liying Wang، نويسنده , , Lei Chen، نويسنده , , Feng Deng، نويسنده ,

  • Issue Information
    روزنامه با شماره پیاپی سال 2003
  • Pages
    10
  • From page
    289
  • To page
    298
  • Abstract
    Life is based on l-amino acids and d-sugars rather than the enantiomeric d-amino acids and l-sugars. This broken symmetry is now believed to be a feature of fundamental physics—a result of symmetry-breaking induced by the weak force, which makes one enantiomer slightly more stable than the other. An amplification mechanism based on quantum mechanical tunneling could give rise to a second-order phase transition. In order to understand the transition mechanism, we measured the temperature dependence of 1H CRAMPS solid state NMR and 13C CP/MAS spectra of d- and l-alanine crystals from 295 K through to 220 K. Obvious difference of NMR behaviors between two enantiomers was observed in the phase transition which may be related to one suggested by Salam, caused biochirality among twenty amino acids.
  • Keywords
    Parity violation , 1H-CRAMPS-ssNMR , Phase transition , 13C-CP/MAS-ssNMR , Alanine enantiomer , Parity-violating energy difference
  • Journal title
    Biophysical Chemistry
  • Serial Year
    2003
  • Journal title
    Biophysical Chemistry
  • Record number

    1113223