Observation of subtle dynamic transitions by a combination of neutron scattering, X-ray diffraction and DSC: A case study of the monoclinic l-cysteine

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Observation of subtle dynamic transitions by a combination of neutron scattering, X-ray diffraction and DSC : A case study of the monoclinic l-cysteine. / Bordallo, Heloisa N.; Boldyreva, Elena V.; Fischer, Jennifer; Koza, Michael Marek; Seydel, Tilo; Minkov, Vasily S.; Drebushchak, Valery A.; Kyriakopoulos, Antonios.

In: Biophysical Chemistry, Vol. 148, No. 1-3, 01.05.2010, p. 34-41.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Bordallo, HN, Boldyreva, EV, Fischer, J, Koza, MM, Seydel, T, Minkov, VS, Drebushchak, VA & Kyriakopoulos, A 2010, 'Observation of subtle dynamic transitions by a combination of neutron scattering, X-ray diffraction and DSC: A case study of the monoclinic l-cysteine', Biophysical Chemistry, vol. 148, no. 1-3, pp. 34-41. https://doi.org/10.1016/j.bpc.2010.02.003

APA

Bordallo, H. N., Boldyreva, E. V., Fischer, J., Koza, M. M., Seydel, T., Minkov, V. S., Drebushchak, V. A., & Kyriakopoulos, A. (2010). Observation of subtle dynamic transitions by a combination of neutron scattering, X-ray diffraction and DSC: A case study of the monoclinic l-cysteine. Biophysical Chemistry, 148(1-3), 34-41. https://doi.org/10.1016/j.bpc.2010.02.003

Vancouver

Bordallo HN, Boldyreva EV, Fischer J, Koza MM, Seydel T, Minkov VS et al. Observation of subtle dynamic transitions by a combination of neutron scattering, X-ray diffraction and DSC: A case study of the monoclinic l-cysteine. Biophysical Chemistry. 2010 May 1;148(1-3):34-41. https://doi.org/10.1016/j.bpc.2010.02.003

Author

Bordallo, Heloisa N. ; Boldyreva, Elena V. ; Fischer, Jennifer ; Koza, Michael Marek ; Seydel, Tilo ; Minkov, Vasily S. ; Drebushchak, Valery A. ; Kyriakopoulos, Antonios. / Observation of subtle dynamic transitions by a combination of neutron scattering, X-ray diffraction and DSC : A case study of the monoclinic l-cysteine. In: Biophysical Chemistry. 2010 ; Vol. 148, No. 1-3. pp. 34-41.

Bibtex

@article{e51de547e2474c6899d7f1819fc4d817,
title = "Observation of subtle dynamic transitions by a combination of neutron scattering, X-ray diffraction and DSC: A case study of the monoclinic l-cysteine",
abstract = "The palper illustrates the benefit of combining several experimental techniques (incoherent elastic and inelastic neutron scattering, DSC, and X-ray diffraction) to study subtle dynamic transitions in a biologically important system, probing a broad time (frequency) range of the molecular motions in a wide temperature interval of 2-300K. As a case study the crystalline form (a monoclinic polymorph) of l-cysteine (+NH3-CH(CH2SH)-COO-) - an essential amino acid - has been selected. Crystals of amino acids are widely used to mimic important structural and dynamic features of peptides. The conformational lability of cysteine and the dynamics of the thiol-side chains are known to account for various phase transitions in the crystalline state and for the conformational transitions important for the biological function in the peptides. The effect of temperature on the monoclinic polymorph of l-cysteine, metastable at ambient conditions, has been studied for the first time. A dynamical transition at about 150K, marking a crossover of the molecular fluctuations between harmonic and non-harmonic dynamical regimes, was evidenced by evaluating the evolution of the mean-square displacement obtained from the elastic fixed window approach using the backscattering spectrometer IN10 located at the ILL. Although this transition does not manifest itself in the DSC, it was clearly observed by incoherent inelastic neutron scattering. By analyzing the dynamical susceptibility contribution (χ{"}(ω)) obtained using IN6 also at ILL we were able to evidence another relaxation process at a different time scale. The disordered soft l-cysteine structure has an excess of inelastic scattering at about 3meV, analogous to the {"}boson peak{"} observed in glass-like materials and proteins. High-precision X-ray diffraction has revealed an anomaly in the changes of selected unit cell parameters and volume at about 240K.",
keywords = "Anharmonicity, Crystalline amino acids, Debye model, Hydrogen bonds, Inelastic neutron scattering, Relaxation time",
author = "Bordallo, {Heloisa N.} and Boldyreva, {Elena V.} and Jennifer Fischer and Koza, {Michael Marek} and Tilo Seydel and Minkov, {Vasily S.} and Drebushchak, {Valery A.} and Antonios Kyriakopoulos",
year = "2010",
month = may,
day = "1",
doi = "10.1016/j.bpc.2010.02.003",
language = "English",
volume = "148",
pages = "34--41",
journal = "Biophysical Chemistry",
issn = "0301-4622",
publisher = "Elsevier",
number = "1-3",

}

RIS

TY - JOUR

T1 - Observation of subtle dynamic transitions by a combination of neutron scattering, X-ray diffraction and DSC

T2 - A case study of the monoclinic l-cysteine

AU - Bordallo, Heloisa N.

AU - Boldyreva, Elena V.

AU - Fischer, Jennifer

AU - Koza, Michael Marek

AU - Seydel, Tilo

AU - Minkov, Vasily S.

AU - Drebushchak, Valery A.

AU - Kyriakopoulos, Antonios

PY - 2010/5/1

Y1 - 2010/5/1

N2 - The palper illustrates the benefit of combining several experimental techniques (incoherent elastic and inelastic neutron scattering, DSC, and X-ray diffraction) to study subtle dynamic transitions in a biologically important system, probing a broad time (frequency) range of the molecular motions in a wide temperature interval of 2-300K. As a case study the crystalline form (a monoclinic polymorph) of l-cysteine (+NH3-CH(CH2SH)-COO-) - an essential amino acid - has been selected. Crystals of amino acids are widely used to mimic important structural and dynamic features of peptides. The conformational lability of cysteine and the dynamics of the thiol-side chains are known to account for various phase transitions in the crystalline state and for the conformational transitions important for the biological function in the peptides. The effect of temperature on the monoclinic polymorph of l-cysteine, metastable at ambient conditions, has been studied for the first time. A dynamical transition at about 150K, marking a crossover of the molecular fluctuations between harmonic and non-harmonic dynamical regimes, was evidenced by evaluating the evolution of the mean-square displacement obtained from the elastic fixed window approach using the backscattering spectrometer IN10 located at the ILL. Although this transition does not manifest itself in the DSC, it was clearly observed by incoherent inelastic neutron scattering. By analyzing the dynamical susceptibility contribution (χ"(ω)) obtained using IN6 also at ILL we were able to evidence another relaxation process at a different time scale. The disordered soft l-cysteine structure has an excess of inelastic scattering at about 3meV, analogous to the "boson peak" observed in glass-like materials and proteins. High-precision X-ray diffraction has revealed an anomaly in the changes of selected unit cell parameters and volume at about 240K.

AB - The palper illustrates the benefit of combining several experimental techniques (incoherent elastic and inelastic neutron scattering, DSC, and X-ray diffraction) to study subtle dynamic transitions in a biologically important system, probing a broad time (frequency) range of the molecular motions in a wide temperature interval of 2-300K. As a case study the crystalline form (a monoclinic polymorph) of l-cysteine (+NH3-CH(CH2SH)-COO-) - an essential amino acid - has been selected. Crystals of amino acids are widely used to mimic important structural and dynamic features of peptides. The conformational lability of cysteine and the dynamics of the thiol-side chains are known to account for various phase transitions in the crystalline state and for the conformational transitions important for the biological function in the peptides. The effect of temperature on the monoclinic polymorph of l-cysteine, metastable at ambient conditions, has been studied for the first time. A dynamical transition at about 150K, marking a crossover of the molecular fluctuations between harmonic and non-harmonic dynamical regimes, was evidenced by evaluating the evolution of the mean-square displacement obtained from the elastic fixed window approach using the backscattering spectrometer IN10 located at the ILL. Although this transition does not manifest itself in the DSC, it was clearly observed by incoherent inelastic neutron scattering. By analyzing the dynamical susceptibility contribution (χ"(ω)) obtained using IN6 also at ILL we were able to evidence another relaxation process at a different time scale. The disordered soft l-cysteine structure has an excess of inelastic scattering at about 3meV, analogous to the "boson peak" observed in glass-like materials and proteins. High-precision X-ray diffraction has revealed an anomaly in the changes of selected unit cell parameters and volume at about 240K.

KW - Anharmonicity

KW - Crystalline amino acids

KW - Debye model

KW - Hydrogen bonds

KW - Inelastic neutron scattering

KW - Relaxation time

UR - http://www.scopus.com/inward/record.url?scp=77951976072&partnerID=8YFLogxK

U2 - 10.1016/j.bpc.2010.02.003

DO - 10.1016/j.bpc.2010.02.003

M3 - Journal article

C2 - 20189291

AN - SCOPUS:77951976072

VL - 148

SP - 34

EP - 41

JO - Biophysical Chemistry

JF - Biophysical Chemistry

SN - 0301-4622

IS - 1-3

ER -

ID: 199168078