Stability and solubility of proteins from extremophiles

Richard B. Greaves, Jim Warwicker

    Research output: Contribution to journalArticlepeer-review


    Charges are important for hyperthermophile protein structure and function. However, the number of charges and their predicted contributions to folded state stability are not correlated, implying that more charge does not imply greater stability. The charge properties that distinguish hyperthermophile proteins also differentiate psychrophile proteins from mesophile proteins, but in the opposite direction and to a smaller extent. We conclude that charge number relates to solubility, whereas protein stability is determined by charge location. Most other structural properties are poorly separated over the ambient temperature range, apart from the burial of certain amino acids. Of particular interest are large non-polar sidechains that tend to increased exposure in proteins evolved to function at higher temperatures. Looking at tryptophan in more detail, this increase is often located close to the termini of secondary structure elements, and is discussed in terms of a novel potential role in protein thermostabilisation. © 2009 Elsevier Inc. All rights reserved.
    Original languageEnglish
    Pages (from-to)581-585
    Number of pages4
    JournalBiochemical and Biophysical Research Communications
    Issue number3
    Publication statusPublished - 13 Mar 2009


    • Charge interactions
    • Extremophiles
    • Protein structure
    • Solubility
    • Sugar binding
    • Thermostability


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