High-pressure Raman spectra ofL-threonine crystal

Silva, B. L.; Freire, Paulo; Melo, F. E. A.; Fílho, J. Mendes; Pimenta, M. A.; Dantas, M. S. S.

doi:10.1002/1097-4555(200006)31:6<519::aid-jrs567>3.0.co;2-x

Cited by 37 publications

(23 citation statements)

References 14 publications

(11 reference statements)

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“…This occurs between 110 and 220 K. This effect can be related to a change in the conformation of the L-arginine molecule in the crystal. A similar phenomenon was observed in the L-threonine single crystal at high pressure, 11 where bands between 300 and 500 cm 1 show a decrease in intensity with increase in pressure. The conformation change in the L-arginine molecule can be facilitated by the fact that the molecule has a relatively long carbonic chain.…”

Section: Resultssupporting

confidence: 76%

“…However, the Raman scattering experiment, through the observation of changes in the low-wavenumber region (<170 cm 1 ), has been found to be a sensitive probe of phase transitions in amino acid crystals. 8,9,11,15 Figure 4 shows the Raman spectra of LAHCL in the x zz x scattering geometry ( < 135 cm 1 ) taken at four different temperatures. Figure 4(a) shows the Raman spectra between 130 and 170 cm 1 .…”

Section: Resultsmentioning

confidence: 99%

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Temperature‐dependent Raman study of L‐arginine hydrochloride monohydrate single crystal

Lima

Freire

Sasaki

et al. 2002

J Raman Spectroscopy

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Polarized Raman spectra of L-arginine hydrochloride monohydrate single crystal were studied at temperatures ranging from 295 to 10 K. The behavior of the linewidth, wavenumber and intensity of several bands is discussed and related to some particular vibrational modes associated with hydrogen bonds or even to other vibrations, such as CN, CCC, CCN and CH vibrations. The disappearance of some bands in the lattice vibrational region was associated with a phase transition undergone by the crystal between 100 and 110 K.

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Section: Resultssupporting

confidence: 76%

Section: Resultsmentioning

confidence: 99%

Temperature‐dependent Raman study of L‐arginine hydrochloride monohydrate single crystal

Lima

Freire

Sasaki

et al. 2002

J Raman Spectroscopy

Self Cite

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“…The amino acids studied to date under pressure reveal some modifications in the internal mode region, mainly discontinuous jumps across the transition, as observed for Lalanine, 5 L-threonine, 13 DL-valine, 16 andˇ-glycine. 7 In the present work for L-methionine, besides discontinuity in the ω vs P plots for the internal modes, the vanishing of strong bands and the appearance of other strong features were observed.…”

Section: Resultsmentioning

confidence: 88%

“…10 -12 Raman spectroscopic studies of L-threonine and taurine, which is a nonproteic amino acid, revealed vibrational and structural changes at ¾2.1 and 0.7 GPa, respectively. 13,14 L-serine, DL-serine, and L-cysteine were also investigated by several authors who report on changes in their structures being observed under high-pressure conditions. 15 -23 Although there is abundance of data on some of the amino acid crystals, many others, with their specific conformation and hydrogen bond network, have not yet been investigated.…”

Section: Introductionmentioning

confidence: 99%

High pressure Raman spectra of L‐methionine crystal

Lima

Freire

Melo

et al. 2008

J Raman Spectroscopy

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Raman spectra of an L-methionine (C 5 H 11 NO 2 S) crystal were obtained in the spectral region between 50 and 3200 cm −1 for pressures up to 5 GPa. Pronounced changes of the Raman spectra were observed for bands associated to rocking of CO 2 − ; wagging of CO 2 − ; deformations of CO 2 − , CH 3 , and NH 3 + ; and stretching vibrations of SC, CC, CH, CH 2 , and CH 3 . Upon decompression to ambient pressure the original Raman spectrum prior to compression is recovered. These modifications were associated to a reversible phase transition undergone by the L-methionine crystal at about 2.2 GPa, with a hysteresis of ∼0.8 GPa. Pressure coefficients for most of the internal modes of the crystal are given.

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“…It is worth to note that the phase transitions in the orthorhombic L-cysteine involve changes in molecular conformation while the pressure-induced phase transitions in the monoclinic phase are mainly related to changes in the hydrogen bond network (Minkov et al, 2010). L-threonine (C 4 H 9 NO 3 ) (Silva et al, 2000) was investigated up to 4.3 GPa through Raman spectroscopy. From this study it was observed several modifications in the Raman spectrum, including the region associated to the lattice mode vibrations, mainly between 2 and 2.2 GPa.…”

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confidence: 99%