A systematic comparative analysis of 21 psychrophilic enzymes belonging to different structural families from pokaryotic and eukaryotic organisms is reported. Our results show a clear tendency for the charged residues Arg and Glu to be replaced at exposed sites on alpha-helices by Lys and Ala, respectively, in the direction from "hot" to "cold" enzymes. Possible implications of the observed structural variations for protein stability and engineering are discussed.
Structural adaptation of enzymes to low temperatures / Pascarella, Stefano; Gianese, Giulio. - In: PROTEIN SCIENCE. - ISSN 0961-8368. - STAMPA. - 10:Supplement 1(2001), pp. 142-142. (Intervento presentato al convegno Fourth European Symposium of the Protein Society tenutosi a Parigi nel 18-22 aprile 2001).
Structural adaptation of enzymes to low temperatures
PASCARELLA, Stefano;GIANESE, Giulio
2001
Abstract
A systematic comparative analysis of 21 psychrophilic enzymes belonging to different structural families from pokaryotic and eukaryotic organisms is reported. Our results show a clear tendency for the charged residues Arg and Glu to be replaced at exposed sites on alpha-helices by Lys and Ala, respectively, in the direction from "hot" to "cold" enzymes. Possible implications of the observed structural variations for protein stability and engineering are discussed.| File | Dimensione | Formato | |
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