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Protein stability and molecular adaptation to extreme conditions

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EJB Reviews 1991

Part of the book series: EJB Reviews 1991 ((EJB REVIEWS,volume 1991))

Abstract

Proteins, due to the delicate balance of stabilizing and destabilizing interactions, are only marginally stable. Adaptation to extreme environments tends to shift the ‘mesophilic’ characteristics of proteins to the respective extremes of temperature, hydrostatic pressure, pH and salinity, such that, under the mutual physiological conditions, the molecular properties are similar regarding overall topology, flexibility and solvation. Enhanced intrinsic stability requires only minute local structural changes so that general strategies of stabilization cannot be established. Apart from mutative changes of amino-acid sequences, extrinsic factors (or cellular components) may be involved in ‘extremophilic adaptation’.

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Abbreviations

BPTI:

basic pancreatic trypsin inhibitor

GAPDH:

glyceraldehyde-3-phosphate dehydrogenase

H-bond:

hydrogen bond

N, U:

native and unfolded states, respectively

RNase:

ribonuclease

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  1. Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, Federal Republic of Germany

    Rainer Jaenicke

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  1. Biochemisches Institut der Universität Zürich, Winterthurerstrasse 190, CH-8057, Zürich, Switzerland

    P. Christen

  2. Institut für Biochemie der Universität Leipzig, Liebigstraße 16, O-7010, Leipzig, Germany

    E. Hofmann

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Jaenicke, R. (1991). Protein stability and molecular adaptation to extreme conditions. In: Christen, P., Hofmann, E. (eds) EJB Reviews 1991. EJB Reviews 1991, vol 1991. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-77200-9_22

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