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


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Article Info

DATE

2000-05-01

AUTHORS

Dieter Perl, Uwe Mueller, Udo Heinemann, Franz X. Schmid

ABSTRACT

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 degrees 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. More... »

PAGES

nsb0500_380

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/75151

DOI

http://dx.doi.org/10.1038/75151

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1013031441

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/10802734


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