Anomalous temperature dependence of the thermal expansion of proteins.
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 x 10(-4) K-1 for a 10% solution.
Hiebl
M
M
Technische Universität München, Physik Department, Garching, Germany.
Maksymiw
R
R
D000818:Animals; D002645:Chickens; D003720:Densitometry; D004531:Eggs; D006863:Hydrogen-Ion Concentration; D008433:Mathematics; D009113:Muramidase / Q000737:chemistry*; D010047:Ovalbumin / Q000737:chemistry*; D011487:Protein Conformation; D012995:Solubility; D013696:Temperature
D010047:Ovalbumin; D009113:Muramidase