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
Link To Document :
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