%0 Journal Article %1 WOS:000246341300002 %A de Souza, Joelma M %A Freire, Paulo T C %A Bordallo, Heloisa N %A Argyriou, Dimitri N %C 1155 16TH ST, NW, WASHINGTON, DC 20036 USA %D 2007 %I AMER CHEMICAL SOC %J JOURNAL OF PHYSICAL CHEMISTRY B %K imported %N 19 %P 5034-5039 %R 10.1021/jp070366z %T Structural isotopic effects in the smallest chiral amino acid: Observation of a structural phase transition in fully deuterated alanine %V 111 %X A first study of possible changes instigated by deuteration in amino acids was carried out using neutron diffraction, inelastic neutron scattering, and Raman scattering in L-alanine, C2H4(NH2)COOH. Careful analysis of the structural parameters shows that deuteration of L-alanine engenders significant geometric changes as a function of temperature, which can be directly related to the observation of new lattice vibration modes in the Raman spectra. The combination of the experimental data suggests that C2D4(ND2)COOD undergoes a structural phase transition (or a structural rearrangement) at about 170 K. Considering that this particular amino acid is a hydrogen-bonded system with short hydrogen bonds (O center dot center dot center dot H similar to 1.8 angstrom), we evoke the Ubbelohde effect to conclude that substitution of hydrogen for deuterium gives rise to changes in the hydrogen-bonding interactions. The structural differences suggest distinct relative stabilities for the hydrogenous and deuterated L-alanine.

@article{WOS:000246341300002, abstract = {A first study of possible changes instigated by deuteration in amino acids was carried out using neutron diffraction, inelastic neutron scattering, and Raman scattering in L-alanine, C2H4(NH2)COOH. Careful analysis of the structural parameters shows that deuteration of L-alanine engenders significant geometric changes as a function of temperature, which can be directly related to the observation of new lattice vibration modes in the Raman spectra. The combination of the experimental data suggests that C2D4(ND2)COOD undergoes a structural phase transition (or a structural rearrangement) at about 170 K. Considering that this particular amino acid is a hydrogen-bonded system with short hydrogen bonds (O center dot center dot center dot H similar to 1.8 angstrom), we evoke the Ubbelohde effect to conclude that substitution of hydrogen for deuterium gives rise to changes in the hydrogen-bonding interactions. The structural differences suggest distinct relative stabilities for the hydrogenous and deuterated L-alanine.}, added-at = {2022-05-23T20:00:14.000+0200}, address = {1155 16TH ST, NW, WASHINGTON, DC 20036 USA}, author = {de Souza, Joelma M and Freire, Paulo T C and Bordallo, Heloisa N and Argyriou, Dimitri N}, biburl = {https://www.bibsonomy.org/bibtex/231be407cff50ca326d4b74148174079e/ppgfis_ufc_br}, doi = {10.1021/jp070366z}, interhash = {02966dbc78e1b1d46c2d17980419fe4f}, intrahash = {31be407cff50ca326d4b74148174079e}, issn = {1520-6106}, journal = {JOURNAL OF PHYSICAL CHEMISTRY B}, keywords = {imported}, number = 19, pages = {5034-5039}, publisher = {AMER CHEMICAL SOC}, pubstate = {published}, timestamp = {2022-05-23T20:00:14.000+0200}, title = {Structural isotopic effects in the smallest chiral amino acid: Observation of a structural phase transition in fully deuterated alanine}, tppubtype = {article}, volume = 111, year = 2007 }