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Free energy change during the formation of crystalline contact between lysozyme monomers under different physical and chemical conditions. / Kordonskaya, Yuliya V.; Timofeev, Vladimir I.; Dyakova, Yulia A.; Marchenkova, Margarita A.; Pisarevsky, Yury V.; Kovalchuk, Mikhail V.

In: Crystals, Vol. 11, No. 9, 1121, 14.09.2021.

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

Harvard

Kordonskaya, YV, Timofeev, VI, Dyakova, YA, Marchenkova, MA, Pisarevsky, YV & Kovalchuk, MV 2021, 'Free energy change during the formation of crystalline contact between lysozyme monomers under different physical and chemical conditions', Crystals, vol. 11, no. 9, 1121. https://doi.org/10.3390/cryst11091121

APA

Kordonskaya, Y. V., Timofeev, V. I., Dyakova, Y. A., Marchenkova, M. A., Pisarevsky, Y. V., & Kovalchuk, M. V. (2021). Free energy change during the formation of crystalline contact between lysozyme monomers under different physical and chemical conditions. Crystals, 11(9), [1121]. https://doi.org/10.3390/cryst11091121

Vancouver

Kordonskaya YV, Timofeev VI, Dyakova YA, Marchenkova MA, Pisarevsky YV, Kovalchuk MV. Free energy change during the formation of crystalline contact between lysozyme monomers under different physical and chemical conditions. Crystals. 2021 Sep 14;11(9). 1121. https://doi.org/10.3390/cryst11091121

Author

Kordonskaya, Yuliya V. ; Timofeev, Vladimir I. ; Dyakova, Yulia A. ; Marchenkova, Margarita A. ; Pisarevsky, Yury V. ; Kovalchuk, Mikhail V. / Free energy change during the formation of crystalline contact between lysozyme monomers under different physical and chemical conditions. In: Crystals. 2021 ; Vol. 11, No. 9.

BibTeX

@article{27c4146758604805a788bbb24b606611,
title = "Free energy change during the formation of crystalline contact between lysozyme monomers under different physical and chemical conditions",
abstract = "We use the MM/GBSA method to calculate the free energies of dimer formation by binding two monomers with different combinations of precipitant ions, both embedded in the structure of monomers and in the crystallization solution. It shows that the largest difference in free energy values corresponds to the most accurate dimer model, which considers all precipitant ions in their structure. In addition, it shows that in the absence of precipitant ions in the solution of lysozyme molecules, a monomer is a more energetically favorable state.",
keywords = "Molecular dynamics, Molecular modeling, Protein crystallography, protein crystallography, GENERALIZED BORN MODEL, MOLECULAR-DYNAMICS, molecular modeling, STAGE, X-RAY-SCATTERING, molecular dynamics, PROTEINS",
author = "Kordonskaya, {Yuliya V.} and Timofeev, {Vladimir I.} and Dyakova, {Yulia A.} and Marchenkova, {Margarita A.} and Pisarevsky, {Yury V.} and Kovalchuk, {Mikhail V.}",
note = "Publisher Copyright: {\textcopyright} 2021 by the authors. Licensee MDPI, Basel, Switzerland.",
year = "2021",
month = sep,
day = "14",
doi = "10.3390/cryst11091121",
language = "English",
volume = "11",
journal = "Liquid Crystals Today",
issn = "1358-314X",
publisher = "MDPI AG",
number = "9",

}

RIS

TY - JOUR

T1 - Free energy change during the formation of crystalline contact between lysozyme monomers under different physical and chemical conditions

AU - Kordonskaya, Yuliya V.

AU - Timofeev, Vladimir I.

AU - Dyakova, Yulia A.

AU - Marchenkova, Margarita A.

AU - Pisarevsky, Yury V.

AU - Kovalchuk, Mikhail V.

N1 - Publisher Copyright: © 2021 by the authors. Licensee MDPI, Basel, Switzerland.

PY - 2021/9/14

Y1 - 2021/9/14

N2 - We use the MM/GBSA method to calculate the free energies of dimer formation by binding two monomers with different combinations of precipitant ions, both embedded in the structure of monomers and in the crystallization solution. It shows that the largest difference in free energy values corresponds to the most accurate dimer model, which considers all precipitant ions in their structure. In addition, it shows that in the absence of precipitant ions in the solution of lysozyme molecules, a monomer is a more energetically favorable state.

AB - We use the MM/GBSA method to calculate the free energies of dimer formation by binding two monomers with different combinations of precipitant ions, both embedded in the structure of monomers and in the crystallization solution. It shows that the largest difference in free energy values corresponds to the most accurate dimer model, which considers all precipitant ions in their structure. In addition, it shows that in the absence of precipitant ions in the solution of lysozyme molecules, a monomer is a more energetically favorable state.

KW - Molecular dynamics

KW - Molecular modeling

KW - Protein crystallography

KW - protein crystallography

KW - GENERALIZED BORN MODEL

KW - MOLECULAR-DYNAMICS

KW - molecular modeling

KW - STAGE

KW - X-RAY-SCATTERING

KW - molecular dynamics

KW - PROTEINS

UR - http://www.scopus.com/inward/record.url?scp=85115809750&partnerID=8YFLogxK

UR - https://www.mendeley.com/catalogue/696b1ae3-970f-32ba-8388-46976e4401f3/

U2 - 10.3390/cryst11091121

DO - 10.3390/cryst11091121

M3 - Article

AN - SCOPUS:85115809750

VL - 11

JO - Liquid Crystals Today

JF - Liquid Crystals Today

SN - 1358-314X

IS - 9

M1 - 1121

ER -

ID: 88195382