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The Journal of Chemical Physics : Intrinsic thermal expansivity and hydrational properties of amyloid peptide Aß42 in liquid water

By I. Brovchenko, R. R. Burri, A. Krukau, A. Oleinikova, and R. Winter

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Book Id: WPLBN0002169528
Format Type: PDF eBook :
File Size: Serial Publication
Reproduction Date: 17 November 2008

Title: The Journal of Chemical Physics : Intrinsic thermal expansivity and hydrational properties of amyloid peptide Aß42 in liquid water  
Author: I. Brovchenko, R. R. Burri, A. Krukau, A. Oleinikova, and R. Winter
Volume: Issue : November 2008
Language: English
Subject: Science, Physics, Natural Science
Collections: Periodicals: Journal and Magazine Collection (Contemporary), The Journal of Chemical Physics Collection
Historic
Publication Date:
Publisher: American Institute of Physics

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R. R. Burri, A. Krukau, A. Oleinikova, And R. Winte, I. B. (n.d.). The Journal of Chemical Physics : Intrinsic thermal expansivity and hydrational properties of amyloid peptide Aß42 in liquid water. Retrieved from http://worldebookfair.com/


Description
Description: Volumetric and conformational properties of the amyloid β(1–42) peptide (Aβ42) are studied in relation to the properties of hydration water in a wide temperature range by computer simulations. The apparent volume of Aβ42, which is the change in the total volume of the solution due to the presence of Aβ42, shows a quite different temperature dependence below and above T ≈ 320 K. The apparent thermal expansion coefficient αapp(Aβ42) is about 1.5×10−3 K−1 at T ≤ 320 K and about 0.6×10−3 K−1 at T>320 K. By evaluation of the thermal expansivity of hydration water, the intrinsic expansivity of the biomolecule in liquid water was determined for the first time. The intrinsic thermal expansion coefficient of Aβ42 is found to be negative: αint(Aβ42) ≈ −0.8×10−3 K−1. The negative thermal expansion coefficient of Aβ42 can be attributed to its rubberlike (entropic) elasticity and/or to a decreasing number of intrapeptide hydrogen bonds. Upon heating, Aβ42 transforms from an extended chain with a significant content of α-helices to a compact coil with noticeable content of β-structures. A hydrogen-bonded spanning network of hydration water envelops Aβ42 homogeneously at low temperatures but breaks into an ensemble of small water clusters upon heating via a percolation transition, whose midpoint is close to the temperature, where the apparent volume of Aβ42 changes its temperature behavior. The mutual relation between the volumetric properties of Aβ42, its conformational properties, and the properties of the hydration water is discussed.

 

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