Structural isotopic effects in the smallest chiral amino acid: Observation of a structural phase transition in fully deuterated alanine

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Standard

Structural isotopic effects in the smallest chiral amino acid : Observation of a structural phase transition in fully deuterated alanine. / De Souza, Joelma M.; Freire, Paulo T.C.; Bordallo, Heloisa N.; Argyriou, Dimitri N.

I: Journal of Physical Chemistry B, Bind 111, Nr. 19, 17.05.2007, s. 5034-5039.

Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › fagfællebedømt

Harvard

De Souza, JM, Freire, PTC, Bordallo, HN & Argyriou, DN 2007, 'Structural isotopic effects in the smallest chiral amino acid: Observation of a structural phase transition in fully deuterated alanine', Journal of Physical Chemistry B, bind 111, nr. 19, s. 5034-5039. https://doi.org/10.1021/jp070366z

APA

De Souza, J. M., Freire, P. T. C., Bordallo, H. N., & Argyriou, D. N. (2007). Structural isotopic effects in the smallest chiral amino acid: Observation of a structural phase transition in fully deuterated alanine. Journal of Physical Chemistry B, 111(19), 5034-5039. https://doi.org/10.1021/jp070366z

Vancouver

De Souza JM, Freire PTC, Bordallo HN, Argyriou DN. Structural isotopic effects in the smallest chiral amino acid: Observation of a structural phase transition in fully deuterated alanine. Journal of Physical Chemistry B. 2007 maj 17;111(19):5034-5039. https://doi.org/10.1021/jp070366z

Author

De Souza, Joelma M. ; Freire, Paulo T.C. ; Bordallo, Heloisa N. ; Argyriou, Dimitri N. / Structural isotopic effects in the smallest chiral amino acid : Observation of a structural phase transition in fully deuterated alanine. I: Journal of Physical Chemistry B. 2007 ; Bind 111, Nr. 19. s. 5034-5039.

Bibtex

@article{abd5891eacdb4140b66643bc38c8e0cd,
title = "Structural isotopic effects in the smallest chiral amino acid: Observation of a structural phase transition in fully deuterated alanine",
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 C2(ND4)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⋯H ∼ 1.8 A), 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.",
author = "{De Souza}, {Joelma M.} and Freire, {Paulo T.C.} and Bordallo, {Heloisa N.} and Argyriou, {Dimitri N.}",
year = "2007",
month = may,
day = "17",
doi = "10.1021/jp070366z",
language = "English",
volume = "111",
pages = "5034--5039",
journal = "Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "19",

}

RIS

TY - JOUR

T1 - Structural isotopic effects in the smallest chiral amino acid

T2 - Observation of a structural phase transition in fully deuterated alanine

AU - De Souza, Joelma M.

AU - Freire, Paulo T.C.

AU - Bordallo, Heloisa N.

AU - Argyriou, Dimitri N.

PY - 2007/5/17

Y1 - 2007/5/17

N2 - 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 C2(ND4)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⋯H ∼ 1.8 A), 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.

AB - 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 C2(ND4)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⋯H ∼ 1.8 A), 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.

UR - http://www.scopus.com/inward/record.url?scp=34249776093&partnerID=8YFLogxK

U2 - 10.1021/jp070366z

DO - 10.1021/jp070366z

M3 - Journal article

AN - SCOPUS:34249776093

VL - 111

SP - 5034

EP - 5039

JO - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

JF - Journal of Physical Chemistry Part B: Condensed Matter, Materials, Surfaces, Interfaces & Biophysical

SN - 1520-6106

IS - 19

ER -

ID: 209601039