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Title: Hydrogen bonds in crystalline D-alanine: diffraction and spectroscopic evidence for differences between enantiomers

Abstract

Enantiomeric amino acids have specific physiological functions in complex biological systems. Systematic studies focusing on the solid-state properties of D-amino acids are, however, still limited. To shed light on this field, structural and spectroscopic studies of D-alanine using neutron powder diffraction, polarized Raman scattering and ab initio calculations of harmonic vibrational frequencies were carried out. Clear changes in the number of vibrational modes are observed as a function of temperature, which can be directly connected to variations of the N—D bond lengths. These results reveal dissimilarities in the structural properties of D-alanine compared with L-alanine.

Authors:
ORCiD logo [1];  [2];  [3];  [4]; ORCiD logo [5]; ORCiD logo [6]
  1. Univ. Federal do Para, Para (Brazil); Univ. Federal do Ceara, Ceara (Brazil)
  2. Univ. of Copenhagen, Copenhagen (Denmark)
  3. Univ. Federal do Ceara, Ceara (Brazil)
  4. European Spallation Source, Lund (Sweden)
  5. Univ. of South Florida, Tampa, FL (United States); Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
  6. Univ. of Copenhagen, Copenhagen (Denmark); Univ. of South Florida, Tampa, FL (United States)
Publication Date:
Research Org.:
Los Alamos National Lab. (LANL), Los Alamos, NM (United States)
Sponsoring Org.:
Universities/Institutions; USDOE
OSTI Identifier:
1413544
Report Number(s):
LA-UR-17-21082
Journal ID: ISSN 2052-2525; IUCRAJ
Grant/Contract Number:
AC52-06NA25396; AC02-05CH11231
Resource Type:
Journal Article: Published Article
Journal Name:
IUCrJ
Additional Journal Information:
Journal Volume: 5; Journal Issue: 1; Journal ID: ISSN 2052-2525
Publisher:
International Union of Crystallography
Country of Publication:
United States
Language:
English
Subject:
37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Biological Science; Inorganic and Physical Chemistry; chirality; structure analysis; configurational change; density-functional-theory-based methods; phase transitions; intermolecular interactions; properties of solids; hydrogen bonding; materials science

Citation Formats

Belo, Ezequiel A., Pereira, Jose E. M., Freire, Paulo T. C., Argyriou, Dimitri N., Eckert, Juergen, and Bordallo, Heloisa N. Hydrogen bonds in crystalline D-alanine: diffraction and spectroscopic evidence for differences between enantiomers. United States: N. p., 2018. Web. doi:10.1107/S2052252517015573.
Belo, Ezequiel A., Pereira, Jose E. M., Freire, Paulo T. C., Argyriou, Dimitri N., Eckert, Juergen, & Bordallo, Heloisa N. Hydrogen bonds in crystalline D-alanine: diffraction and spectroscopic evidence for differences between enantiomers. United States. doi:10.1107/S2052252517015573.
Belo, Ezequiel A., Pereira, Jose E. M., Freire, Paulo T. C., Argyriou, Dimitri N., Eckert, Juergen, and Bordallo, Heloisa N. 2018. "Hydrogen bonds in crystalline D-alanine: diffraction and spectroscopic evidence for differences between enantiomers". United States. doi:10.1107/S2052252517015573.
@article{osti_1413544,
title = {Hydrogen bonds in crystalline D-alanine: diffraction and spectroscopic evidence for differences between enantiomers},
author = {Belo, Ezequiel A. and Pereira, Jose E. M. and Freire, Paulo T. C. and Argyriou, Dimitri N. and Eckert, Juergen and Bordallo, Heloisa N.},
abstractNote = {Enantiomeric amino acids have specific physiological functions in complex biological systems. Systematic studies focusing on the solid-state properties of D-amino acids are, however, still limited. To shed light on this field, structural and spectroscopic studies of D-alanine using neutron powder diffraction, polarized Raman scattering and ab initio calculations of harmonic vibrational frequencies were carried out. Clear changes in the number of vibrational modes are observed as a function of temperature, which can be directly connected to variations of the N—D bond lengths. These results reveal dissimilarities in the structural properties of D-alanine compared with L-alanine.},
doi = {10.1107/S2052252517015573},
journal = {IUCrJ},
number = 1,
volume = 5,
place = {United States},
year = 2018,
month = 1
}

Journal Article:
Free Publicly Available Full Text
Publisher's Version of Record at 10.1107/S2052252517015573

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  • Enantiomeric amino acids have specific physiological functions in complex biological systems. Systematic studies focusing on the solid-state properties of D-amino acids are, however, still limited. To shed light on this field, structural and spectroscopic studies of D-alanine using neutron powder diffraction, polarized Raman scattering and ab initio calculations of harmonic vibrational frequencies were carried out. Clear changes in the number of vibrational modes are observed as a function of temperature, which can be directly connected to variations of the N—D bond lengths. These results reveal dissimilarities in the structural properties of D-alanine compared with L-alanine.
  • The low-frequency shoulder of the OH stretching Raman spectrum is developed as a probe of in-phase collective motions in liquid water. Its relative intensity approaches that of ice I as the supercooled liquid temperature tends toward the conjectured thermodynamic singularity in the vicinity of -46/sup 0/C. The collective band appears despite the large disorder of the OH stretching frequencies in the liquid compared to the strength of the resonance coupling. The resonance condition required for collective OH motions leads us to conjecture that patches of water molecules with similar hydrogen bond energies, which are capable of sustaining the resonance, appearmore » as water is supercooled toward T/sub s/.« less
  • Single crystal neutron diffraction has been used in an investigation of the structures of the amino acids L- and D-alanine. The aim of the study was to look for proposed phase transitions around T{sub c} {approx} 270 K. Measurements of both structures at 295 K and 60 K - the neutron structure of D-alanine being determined for the first time - show no significant structural basis for this phase transition in alanine. Further, confirmatory, investigation of the structure of D-alanine at temperatures of 240, 250, 260 and 300 K also showed no significant changes in bond lengths or angles. Wemore » can thus offer no structural support to other physical measurements, which are indicative of the observable effect of parity violation of the electroweak force in these phase transitions.« less
  • No abstract prepared.