Corrigendum: Trading off stability against activity in extremophilic aldolases

@inproceedings{Dick2016CorrigendumTO,
  title={Corrigendum: Trading off stability against activity in extremophilic aldolases},
  author={Markus Dick and Oliver H. Weiergr{\"a}ber and Thomas Classen and Carolin Bisterfeld and Julia Bramski and Holger Gohlke and J{\"o}rg Pietruszka},
  booktitle={Scientific reports},
  year={2016}
}
Understanding enzyme stability and activity in extremophilic organisms is of great biotechnological interest, but many questions are still unsolved. Using 2-deoxy-D-ribose-5-phosphate aldolase (DERA) as model enzyme, we have evaluated structural and functional characteristics of different orthologs from psychrophilic, mesophilic and hyperthermophilic organisms. We present the first crystal structures of psychrophilic DERAs, revealing a dimeric organization resembling their mesophilic but not… CONTINUE READING

From This Paper

Figures, tables, results, connections, and topics extracted from this paper.
0 Extracted Citations
77 Extracted References
Similar Papers

Referenced Papers

Publications referenced by this paper.
Showing 1-10 of 77 references

Web server and services for comparing protein flexibility

  • Tiwari, S. P. et al. WEBnm@ v2.0
  • BMC Bioinformatics 15, 427
  • 2014

Software for processing and analysis of molecular dynamics trajectory data

  • D. R. Roe, Cheatham, T. E. PTRAJ, CPPTRAJ
  • J. Chem. Theory. Comput. 9, 3084–3095
  • 2013

from folding to function and biotechnology

  • Feller, G. Psychrophilic enzymes
  • Scientifica (Cairo) 2013, 512840
  • 2013

Similar Papers

Loading similar papers…