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Chemicals, plastics and rubber industries

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Thermodynamic properties underlying the alpha-helix-to-beta-sheet transition, aggregation, and amyloidgenesis of polulysine as probed by calorimetry, densimetry, and ultrasound velocimetry

Article Abstract:

A detailed thermodynamic study of an aggregation-prone polypeptide, polylysine, is performed to gain a deeper insight into the scenario of physicochemical events during its unfolding, aggregation, and amyloidogenesis. The precise and simultaneous determination of the partial molar volume, the heat capacity and the coefficients of thermal expansion as well as adiabatic and isothermal compressibility of the protein upon unfolding and aggregation yields a thermodynamic aggregation process highlighting the importance of volume fluctuations during unfolding and amyloidogenesis of proteins.

Author: Winter, Roland, Smirnovas, Vytautas, Funck, Theodor, Dzwolak, Wojciech
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2005
Polypeptides, Polysilicon, Chemical properties

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Thermodynamic properties of the NaCl + H2O system. 4. Heat capacities of H2 and NaCl(aq) in cold-stable and supercooled states

Article Abstract:

The specific heat capacities of water and NaCl(aq) are measured from 280 K to lee than equal to 236 K and for NaCl(aq) compositions from 0.05 to 6 mol.kg(super -1). These measurements are found more accurate than the measurements of heat capacities of water and NaCl(aq) and also probe wider ranges of temperature and composition variables for NaCl(aq).

Author: Archer, Donald G., Carter, Richard W.
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2000
Sodium chloride

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Hydration thermodynamic properties of amino acid analogues: A systematic comparison of biomolecular force fields and water models

Article Abstract:

An extensive study of hydration thermodynamic properties of analogues of 13 amino acid side chains at 298 K and 1 atm is presented. It was found that the choice of water model strongly influences the accuracy of the calculated hydration entropies, enthalpies and heat capacities while differences in accuracy between the force fields are small.

Author: van der Vegt, Nico F.A., Hess, Berk
Publisher: American Chemical Society
Publication Name: Journal of Physical Chemistry B
Subject: Chemicals, plastics and rubber industries
ISSN: 1520-6106
Year: 2006
Amino acids, Hydration (Chemistry)

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Subjects list: Research, Thermal properties, Thermodynamics
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