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Structure–Property Relationship in the Crystals of Chiral Amino Acids and Their Racemic Counterparts Conference Abstracts

Conference XXI International Union of Crystallography Congress
23-31 Aug 2008 , Osaka
Journal Acta Crystallographica Section A: Foundations and Advances (предыдущее название Acta Crystallographica Section A: Foundations of Crystallography)
ISSN: 2053-2733
Output data Year: 2008, Volume: 64, Article number : MS.14.2, Pages count : 2 DOI: 10.1107/s0108767308098929
Tags crystalline amino acids, structure-properties relations, head-to-tail chains
Authors Minkov Vasily S. 1,2 , Boldyreva E.V. 1,2 , Drebushchak T.N. 1,2 , Kolesov B.A. 3 , Chesalov Yu.A. 1,4 , Goryainov S.V. 5 , Paukov I.E. 3 , Chernoby G.B. 1,2 , Bordallo H.N. 6 , Kolesnik E.N. 1,2 , Drebushchak V.A. 1,5
Affiliations
1 Novosibirsk State University, Solid State Chemistry, 1, Pirogova street, Novosibirsk, 630090
2 Institute of solid state chemistry SB RAS, Novosibirsk, Russia
3 Institute of inorganic chemistry SB RAS, Novosibirsk, Russia
4 Boreskov Institute of catalysis SB RAS, Novosibirsk, Russia
5 Institute of geology and mineralogy SB RAS, Novosibirsk, Russia
6 Hahn-Meitner Institute, Berlin, Germany

Funding (5)

1 Siberian Branch of the Russian Academy of Sciences 49
2 Siberian Branch of the Russian Academy of Sciences 110
3 Russian Foundation for Basic Research 05-03-32468
4 Civilian Research and Development Foundation NO-008-XI/BG6108
5 Civilian Research and Development Foundation RUX0-008-NO-06

Abstract: Understanding structure-property relations in crystalline amino acids is an important challenge. The structure-forming units in the crystals of amino acids are similar to those in the biopolymers: robust head-to-tail chains of molecules linked by hydrogen bonds are preserved even on polymorphic transformations. Packing of the head-to-tail chains can mimic polypeptide structures: helical structures, b-sheets, amiloids. Knowledge about the temperature and pressure-induced changes in these crystals can help to understand better the contributions to the dynamic properties of proteins related to the intrinsic motions of structural fragments. Besides, crystalline amino acids are important materials with non-linear optical and piezoelectric properties. The structures and properties of the chiral and racemic crystals of amino acids are remarkably different. In the present contribution we illustrate this using several selected examples (L- and DL-serine, L- and DL-cysteine, L- and DL-alanine, L- and DL-phenylalanine, L- and DL-phenylglycine) studied at variable temperatures (the range 3-450 K) and variable pressures (up to 1-10 GPa, depending on the compound and the technique) by single-crystal and powder X-ray diffraction, IR-, Raman, inelastic neutron scattering spectroscopy, and calorimetry. The differences in the structural response to variations in temperature and pressure (different values of compressibility and thermal expansion, different strain anisotropy, different stability with respect to phase transitions induced by cooling, heating or increasing pressure). The study was supported by Integration projects #49 and #110 of SB RAS, a grant from RFBR (05-03-32468) and grants from BRHE (NO-008-XI and RUX0-008-NO-06).
Cite: Minkov V.S. , Boldyreva E.V. , Drebushchak T.N. , Kolesov B.A. , Chesalov Y.A. , Goryainov S.V. , Paukov I.E. , Chernoby G.B. , Bordallo H.N. , Kolesnik E.N. , Drebushchak V.A.
Structure–Property Relationship in the Crystals of Chiral Amino Acids and Their Racemic Counterparts
Acta Crystallographica Section A: Foundations and Advances (предыдущее название Acta Crystallographica Section A: Foundations of Crystallography). 2008. V.64. MS.14.2 :1-2. DOI: 10.1107/s0108767308098929 WOS РИНЦ OpenAlex
Files: Full text from publisher
Dates:
Published print: Aug 23, 2008
Identifiers:
Web of science: WOS:000480420700107
Elibrary: 30472005
OpenAlex: W2326841175
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