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Structure of Aqueous Solutions of Trimethylaminoxide, Urea, and Their Mixture. / Kadtsyn, E. D.; Anikeenko, A. V.; Medvedev, N. N.

In: Journal of Structural Chemistry, Vol. 59, No. 2, 01.03.2018, p. 347-354.

Research output: Contribution to journal › Article › peer-review

Harvard

Kadtsyn, ED, Anikeenko, AV & Medvedev, NN 2018, 'Structure of Aqueous Solutions of Trimethylaminoxide, Urea, and Their Mixture', Journal of Structural Chemistry, vol. 59, no. 2, pp. 347-354. https://doi.org/10.1134/S0022476618020130

APA

Kadtsyn, E. D., Anikeenko, A. V., & Medvedev, N. N. (2018). Structure of Aqueous Solutions of Trimethylaminoxide, Urea, and Their Mixture. Journal of Structural Chemistry, 59(2), 347-354. https://doi.org/10.1134/S0022476618020130

Vancouver

Kadtsyn ED, Anikeenko AV, Medvedev NN. Structure of Aqueous Solutions of Trimethylaminoxide, Urea, and Their Mixture. Journal of Structural Chemistry. 2018 Mar 1;59(2):347-354. doi: 10.1134/S0022476618020130

Author

Kadtsyn, E. D. ; Anikeenko, A. V. ; Medvedev, N. N. / Structure of Aqueous Solutions of Trimethylaminoxide, Urea, and Their Mixture. In: Journal of Structural Chemistry. 2018 ; Vol. 59, No. 2. pp. 347-354.

BibTeX

@article{db8622a510cf49adb13f1dd67acf9d52,
title = "Structure of Aqueous Solutions of Trimethylaminoxide, Urea, and Their Mixture",
abstract = "Aqueous solutions of natural osmolytes (trimethylaminoxide (TMAO), urea, and their mixture) at relatively small (biologically relevant) concentrations are analyzed by the all-atom molecular dynamics simulation. In the recent work (Smolin N. et al. PCCP. 2017. 19. P. 6345) it has been noted that in the protein hydration shell the fraction of TMAO molecules is much smaller than that of urea. The urea addition causes a further decrease in the TMAO fraction in the protein hydration shell. This work shows that in binary solutions urea fraction at urea molecules is always larger than the bulk urea concentration. At the same time, the TMAO fraction near TMAO is the same as in the bulk. In ternary solutions, TMAO and urea behave the same as the binary ones, i.e. they do not noticeably affect each other. This means that the behavior of TMAO and urea molecules in the protein hydration shell is associated with protein rather than their interaction with each other.",
keywords = "aqueous solutions, denaturants, molecular dynamics simulation, osmolyte protectors, trimethylaminoxide, urea",
author = "Kadtsyn, {E. D.} and Anikeenko, {A. V.} and Medvedev, {N. N.}",
note = "Publisher Copyright: {\textcopyright} 2018, Pleiades Publishing, Ltd.",
year = "2018",
month = mar,
day = "1",
doi = "10.1134/S0022476618020130",
language = "English",
volume = "59",
pages = "347--354",
journal = "Journal of Structural Chemistry",
issn = "0022-4766",
publisher = "Springer GmbH & Co, Auslieferungs-Gesellschaf",
number = "2",

}

RIS

TY - JOUR

T1 - Structure of Aqueous Solutions of Trimethylaminoxide, Urea, and Their Mixture

AU - Kadtsyn, E. D.

AU - Anikeenko, A. V.

AU - Medvedev, N. N.

N1 - Publisher Copyright: © 2018, Pleiades Publishing, Ltd.

PY - 2018/3/1

Y1 - 2018/3/1

N2 - Aqueous solutions of natural osmolytes (trimethylaminoxide (TMAO), urea, and their mixture) at relatively small (biologically relevant) concentrations are analyzed by the all-atom molecular dynamics simulation. In the recent work (Smolin N. et al. PCCP. 2017. 19. P. 6345) it has been noted that in the protein hydration shell the fraction of TMAO molecules is much smaller than that of urea. The urea addition causes a further decrease in the TMAO fraction in the protein hydration shell. This work shows that in binary solutions urea fraction at urea molecules is always larger than the bulk urea concentration. At the same time, the TMAO fraction near TMAO is the same as in the bulk. In ternary solutions, TMAO and urea behave the same as the binary ones, i.e. they do not noticeably affect each other. This means that the behavior of TMAO and urea molecules in the protein hydration shell is associated with protein rather than their interaction with each other.

AB - Aqueous solutions of natural osmolytes (trimethylaminoxide (TMAO), urea, and their mixture) at relatively small (biologically relevant) concentrations are analyzed by the all-atom molecular dynamics simulation. In the recent work (Smolin N. et al. PCCP. 2017. 19. P. 6345) it has been noted that in the protein hydration shell the fraction of TMAO molecules is much smaller than that of urea. The urea addition causes a further decrease in the TMAO fraction in the protein hydration shell. This work shows that in binary solutions urea fraction at urea molecules is always larger than the bulk urea concentration. At the same time, the TMAO fraction near TMAO is the same as in the bulk. In ternary solutions, TMAO and urea behave the same as the binary ones, i.e. they do not noticeably affect each other. This means that the behavior of TMAO and urea molecules in the protein hydration shell is associated with protein rather than their interaction with each other.

KW - aqueous solutions

KW - denaturants

KW - molecular dynamics simulation

KW - osmolyte protectors

KW - trimethylaminoxide

KW - urea

UR - http://www.scopus.com/inward/record.url?scp=85048105565&partnerID=8YFLogxK

U2 - 10.1134/S0022476618020130

DO - 10.1134/S0022476618020130

M3 - Article

AN - SCOPUS:85048105565

VL - 59

SP - 347

EP - 354

JO - Journal of Structural Chemistry

JF - Journal of Structural Chemistry

SN - 0022-4766

IS - 2

ER -

ID: 13794642