The enhanced stability of a cold shock protein from a thermophilic organism, compared to its counterpart from a mesophile, results mainly from a single change in amino acid sequence that improves electrostatic interactions among the charged groups on the protein surface.
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Thermodynamics of protein denaturation at temperatures over 100 °C: CutA1 mutant proteins substituted with hydrophobic and charged residues
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Pace, C. Single surface stabilizer. Nat Struct Mol Biol 7, 345–346 (2000). https://doi.org/10.1038/75100
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DOI: https://doi.org/10.1038/75100
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