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Structure–Property Relationship in the Crystals of Chiral Amino Acids and Their Racemic Counterparts Тезисы доклада

Конференция XXI International Union of Crystallography Congress
23-31 авг. 2008 , Osaka
Журнал Acta Crystallographica Section A: Foundations and Advances (предыдущее название Acta Crystallographica Section A: Foundations of Crystallography)
ISSN: 2053-2733
Вых. Данные Год: 2008, Том: 64, Номер статьи : MS.14.2, Страниц : 2 DOI: 10.1107/s0108767308098929
Ключевые слова crystalline amino acids, structure-properties relations, head-to-tail chains
Авторы 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
Организации
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

Информация о финансировании (5)

1 Сибирское отделение Российской академии наук 49
2 Сибирское отделение Российской академии наук 110
3 Российский фонд фундаментальных исследований 05-03-32468
4 Civilian Research and Development Foundation NO-008-XI/BG6108
5 Civilian Research and Development Foundation RUX0-008-NO-06

Реферат: 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).
Библиографическая ссылка: 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
Файлы: Полный текст от издателя
Даты:
Опубликована в печати: 23 авг. 2008 г.
Идентификаторы БД:
Web of science: WOS:000480420700107
РИНЦ: 30472005
OpenAlex: W2326841175
Цитирование в БД:
БД Цитирований
РИНЦ 1
Web of science 1
OpenAlex 3
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