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Configurational Disorder of Water Hydrogen-Bond Network at the Protein Dynamical Transition

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Configurational Disorder of Water Hydrogen-Bond Network at the Protein Dynamical Transition. / Rahaman, Obaidur; Kalimeri, Maria; Katava, Marina; Paciaroni, Alessandro; Sterpone, Fabio.

In: Journal of Physical Chemistry Part B, Vol. 121, No. 28, 20.07.2017, p. 6792-6798.

Research output: Contribution to journalArticleScientificpeer-review

Harvard

Rahaman, O, Kalimeri, M, Katava, M, Paciaroni, A & Sterpone, F 2017, 'Configurational Disorder of Water Hydrogen-Bond Network at the Protein Dynamical Transition', Journal of Physical Chemistry Part B, vol. 121, no. 28, pp. 6792-6798. https://doi.org/10.1021/acs.jpcb.7b03888

APA

Rahaman, O., Kalimeri, M., Katava, M., Paciaroni, A., & Sterpone, F. (2017). Configurational Disorder of Water Hydrogen-Bond Network at the Protein Dynamical Transition. Journal of Physical Chemistry Part B, 121(28), 6792-6798. https://doi.org/10.1021/acs.jpcb.7b03888

Vancouver

Rahaman O, Kalimeri M, Katava M, Paciaroni A, Sterpone F. Configurational Disorder of Water Hydrogen-Bond Network at the Protein Dynamical Transition. Journal of Physical Chemistry Part B. 2017 Jul 20;121(28):6792-6798. https://doi.org/10.1021/acs.jpcb.7b03888

Author

Rahaman, Obaidur ; Kalimeri, Maria ; Katava, Marina ; Paciaroni, Alessandro ; Sterpone, Fabio. / Configurational Disorder of Water Hydrogen-Bond Network at the Protein Dynamical Transition. In: Journal of Physical Chemistry Part B. 2017 ; Vol. 121, No. 28. pp. 6792-6798.

Bibtex - Download

@article{2c3f9b41afaa4c47af2eee0476b7580f,
title = "Configurational Disorder of Water Hydrogen-Bond Network at the Protein Dynamical Transition",
abstract = "We introduce a novel strategy to quantify the disorder of extended water-water hydrogen-bond (HB) networks sampled in particle-based computer simulations. The method relies on the conformational clustering of the HB connectivity states. We successfully applied it to unveil the fine relationship among the protein dynamical transition in hydrated powder, which marks the activation of protein flexibility at Td ≈ 240 K, and the sudden increase in the configurational disorder of the water HB network enveloping the proteins. Our finding links, in the spirit of the Adam-Gibbs relationship, the diffusivity of protein atoms, as quantified by the hydrogen mean-square displacements, and the thermodynamic solvent configurational entropy.",
author = "Obaidur Rahaman and Maria Kalimeri and Marina Katava and Alessandro Paciaroni and Fabio Sterpone",
year = "2017",
month = "7",
day = "20",
doi = "10.1021/acs.jpcb.7b03888",
language = "English",
volume = "121",
pages = "6792--6798",
journal = "Journal of Physical Chemistry Part B",
issn = "1520-6106",
publisher = "American Chemical Society",
number = "28",

}

RIS (suitable for import to EndNote) - Download

TY - JOUR

T1 - Configurational Disorder of Water Hydrogen-Bond Network at the Protein Dynamical Transition

AU - Rahaman, Obaidur

AU - Kalimeri, Maria

AU - Katava, Marina

AU - Paciaroni, Alessandro

AU - Sterpone, Fabio

PY - 2017/7/20

Y1 - 2017/7/20

N2 - We introduce a novel strategy to quantify the disorder of extended water-water hydrogen-bond (HB) networks sampled in particle-based computer simulations. The method relies on the conformational clustering of the HB connectivity states. We successfully applied it to unveil the fine relationship among the protein dynamical transition in hydrated powder, which marks the activation of protein flexibility at Td ≈ 240 K, and the sudden increase in the configurational disorder of the water HB network enveloping the proteins. Our finding links, in the spirit of the Adam-Gibbs relationship, the diffusivity of protein atoms, as quantified by the hydrogen mean-square displacements, and the thermodynamic solvent configurational entropy.

AB - We introduce a novel strategy to quantify the disorder of extended water-water hydrogen-bond (HB) networks sampled in particle-based computer simulations. The method relies on the conformational clustering of the HB connectivity states. We successfully applied it to unveil the fine relationship among the protein dynamical transition in hydrated powder, which marks the activation of protein flexibility at Td ≈ 240 K, and the sudden increase in the configurational disorder of the water HB network enveloping the proteins. Our finding links, in the spirit of the Adam-Gibbs relationship, the diffusivity of protein atoms, as quantified by the hydrogen mean-square displacements, and the thermodynamic solvent configurational entropy.

U2 - 10.1021/acs.jpcb.7b03888

DO - 10.1021/acs.jpcb.7b03888

M3 - Article

VL - 121

SP - 6792

EP - 6798

JO - Journal of Physical Chemistry Part B

JF - Journal of Physical Chemistry Part B

SN - 1520-6106

IS - 28

ER -