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Anomalous temperature dependence of the thermal expansion of proteins

✍ Scribed by Manfred Hiebl; Roman Maksymiw

Publisher
Wiley (John Wiley & Sons)
Year
1991
Tongue
English
Weight
521 KB
Volume
31
Category
Article
ISSN
0006-3525

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✦ Synopsis

Abstract

The temperature dependence of the apparent expansibility of lysozyme and ovalbumin in Solution has been measured as a function of pH. This temperature dependence is explained in terms of suppressed fluctuations in bound water due to the protein. It is shown that the thermal expansion coefficient of bound water is different from bulk water. The pH dependence can be explained by increased hydration of side chains at lower pH. The amount in volume of hydration water in a typical protein–water system varies from 0.16 to 0.7. How the intrinsic thermal expansion coefficient of proteins can be derived from the apparent quantity is discussed. Intrinsic values of the thermal expansion coefficient for lysozyme at room temperature are between 1.7 and 4.4 Γ— 10^βˆ’4^ K^βˆ’1^ for a 10% solution.

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