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Letter
Nature Structural Biology  7, 380 - 383 (2000)
doi:10.1038/75151

Two exposed amino acid residues confer thermostability on a cold shock protein

Dieter Perl1, Uwe Mueller2, 3, Udo Heinemann2, 3 & Franz X. Schmid1

1  Biochemisches Laboratorium, Universität Bayreuth , D-95440 Bayreuth, Germany.

2  Forschungsgruppe Kristallographie, Max-Delbrück-Centrum für Molekulare Medizin, Robert-Roessle-Str. 10, D-13125 Berlin, Germany.

3  Institut für Chemie − Kristallographie, Freie Universität Berlin, Takustr. 6, D-14195 Berlin, Germany.

Correspondence should be addressed to Franz X. Schmid FX.Schmid@uni-bayreuth.de
Thermophilic organisms produce proteins of exceptional stability. To understand protein thermostability at the molecular level we studied a pair of cold shock proteins, one of mesophilic and one of thermophilic origin, by systematic mutagenesis. Although the two proteins differ in sequence at 12 positions, two surface-exposed residues are responsible for the increase in stability of the thermophilic protein (by 15.8 kJ mol-1 at 70 °C). 11.5 kJ mol-1 originate from a predominantly electrostatic contribution of Arg 3 and 5.2 kJ mol-1 from hydrophobic interactions of Leu 66 at the carboxy terminus. The mesophilic protein could be converted to a highly thermostable form by changing the Glu residues at positions 3 and 66 to Arg and Leu, respectively. The variation of surface residues may thus provide a simple and powerful approach for increasing the thermostability of a protein.


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Nature Structural & Molecular Biology
ISSN: 1545-9993
EISSN: 1545-9985
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