Abstract Water is an indispensable prerequisite for the existence of life. Only in an aqueous environment can biomolecules take up their native, tertiary structure and organize themselves into higher aggregates like multienzyme complexes or cell-organelles. In most of these processes interactions between biomolecules and water play an important role. The influence of pressure and temperature upon intramolecular interactions of biopolymers and biopolymer-water interactions are discussed. Because of fast hydrolysis biomolecules should be unstable at T ⩾ 500 K. Hydrostatic pressure leads to an accelerated hydrolysis. The p, T-dependence of hydrophobic interactions suggest an even lower upper boundary around T ≈ 400 K. In the modelsystem t-butanol/water compression weakens hydrophobic interactions. However, within the modest pressure range p ⩽ 120 MPa observed on earth hydrostatic pressure does not seem to limit the stability of biomolecules at temperatures below 400 K severely.


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    Title :

    Physical-chemical limits for the stability of biomolecules


    Contributors:
    Lang, E.W. (author)

    Published in:

    Advances in Space Research ; 6 , 12 ; 251-255


    Publication date :

    1987-01-01


    Size :

    5 pages




    Type of media :

    Article (Journal)


    Type of material :

    Electronic Resource


    Language :

    English



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