Mobility of Water, Urea and Trimethylamine-N-Oxide Molecules in the Vicinity of Globular Protein

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Mobility of Water, Urea and Trimethylamine-N-Oxide Molecules in the Vicinity of Globular Protein. / Voloshin, V. P.; Medvedev, N. N.

In: Journal of Structural Chemistry, Vol. 60, No. 6, 01.06.2019, p. 942-951.

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

BibTeX

@article{a3f256b4844d422881530c45290daf21,

title = "Mobility of Water, Urea and Trimethylamine-N-Oxide Molecules in the Vicinity of Globular Protein",

abstract = "Molecular mobility in the hydration shell of the SNase globular protein in an aqueous solution with cosolvents (urea and trimethylamine oxide) is studied using all-atom molecular dynamic simulations. Average displacements of the molecules initially located in the successive layers around the protein are calculated over the same short period of time to characterize the diffusion mobility of the molecules depending on the distance to the protein. It is shown that solvent molecules have lower mobility near the protein, and the mobility of more distant molecules increases irregularly and correlates with the positions of the distribution function maxima of these molecules around the protein. After the second maximum of these functions, the mobility reaches its bulky values both for water and the cosolvent.",

keywords = "aqueous solutions, cosolvents, hydration shell, molecular dynamic modeling, trimethylamine-N-oxide, urea",

author = "Voloshin, {V. P.} and Medvedev, {N. N.}",

year = "2019",

month = jun,

day = "1",

doi = "10.1134/S0022476619060088",

language = "English",

volume = "60",

pages = "942--951",

journal = "Journal of Structural Chemistry",

issn = "0022-4766",

publisher = "Springer GmbH & Co, Auslieferungs-Gesellschaf",

number = "6",

}

RIS

TY - JOUR

T1 - Mobility of Water, Urea and Trimethylamine-N-Oxide Molecules in the Vicinity of Globular Protein

AU - Voloshin, V. P.

AU - Medvedev, N. N.

PY - 2019/6/1

Y1 - 2019/6/1

N2 - Molecular mobility in the hydration shell of the SNase globular protein in an aqueous solution with cosolvents (urea and trimethylamine oxide) is studied using all-atom molecular dynamic simulations. Average displacements of the molecules initially located in the successive layers around the protein are calculated over the same short period of time to characterize the diffusion mobility of the molecules depending on the distance to the protein. It is shown that solvent molecules have lower mobility near the protein, and the mobility of more distant molecules increases irregularly and correlates with the positions of the distribution function maxima of these molecules around the protein. After the second maximum of these functions, the mobility reaches its bulky values both for water and the cosolvent.

AB - Molecular mobility in the hydration shell of the SNase globular protein in an aqueous solution with cosolvents (urea and trimethylamine oxide) is studied using all-atom molecular dynamic simulations. Average displacements of the molecules initially located in the successive layers around the protein are calculated over the same short period of time to characterize the diffusion mobility of the molecules depending on the distance to the protein. It is shown that solvent molecules have lower mobility near the protein, and the mobility of more distant molecules increases irregularly and correlates with the positions of the distribution function maxima of these molecules around the protein. After the second maximum of these functions, the mobility reaches its bulky values both for water and the cosolvent.

KW - aqueous solutions

KW - cosolvents

KW - hydration shell

KW - molecular dynamic modeling

KW - trimethylamine-N-oxide

KW - urea

UR - http://www.scopus.com/inward/record.url?scp=85068557301&partnerID=8YFLogxK

U2 - 10.1134/S0022476619060088

DO - 10.1134/S0022476619060088

M3 - Article

AN - SCOPUS:85068557301

VL - 60

SP - 942

EP - 951

JO - Journal of Structural Chemistry

JF - Journal of Structural Chemistry

SN - 0022-4766

IS - 6

ER -

ID: 20780499