Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering

Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by... Mean macromolecular dynamics was quantified in vivo by neutron scattering in psychrophile, mesophile, thermophile and hyperthermophile bacteria. Root mean square atomic fluctuation amplitudes determining macromolecular flexibility were found to be similar for each organism at its physiological temperature (∼1 Å in the 0.1 ns timescale). Effective force constants determining the mean macromolecular resilience were found to increase with physiological temperature from 0.2 N/m for the psychrophiles, which grow at 4°C, to 0.6 N/m for the hyperthermophiles (85°C), indicating that the increase in stabilization free energy is dominated by enthalpic rather than entropic terms. Larger resilience allows macromolecular stability at high temperatures, while maintaining flexibility within acceptable limits for biological activity. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png EMBO Reports Wiley

Adaptation to extreme environments: macromolecular dynamics in bacteria compared in vivo by neutron scattering

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Publisher
Wiley
Copyright
Copyright © 2013 Wiley Periodicals, Inc
ISSN
1469-221X
eISSN
1469-3178
DOI
10.1038/sj.embor.7400049
Publisher site
See Article on Publisher Site

Abstract

Mean macromolecular dynamics was quantified in vivo by neutron scattering in psychrophile, mesophile, thermophile and hyperthermophile bacteria. Root mean square atomic fluctuation amplitudes determining macromolecular flexibility were found to be similar for each organism at its physiological temperature (∼1 Å in the 0.1 ns timescale). Effective force constants determining the mean macromolecular resilience were found to increase with physiological temperature from 0.2 N/m for the psychrophiles, which grow at 4°C, to 0.6 N/m for the hyperthermophiles (85°C), indicating that the increase in stabilization free energy is dominated by enthalpic rather than entropic terms. Larger resilience allows macromolecular stability at high temperatures, while maintaining flexibility within acceptable limits for biological activity.

Journal

EMBO ReportsWiley

Published: Jan 1, 2004

References

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    Bon, C; Lehmann, MS; Wilkinson, C
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    Brooks, CL; Karplus, M; Pettitt, BM
  • A view of dynamics changes in the molten globule‐native folding step by quasielastic neutron scattering
    Bu, Z; Neumann, DA; Lee, SH; Brown, CM; Engelman, DM; Han, CC
  • Dynamic regimes and correlated structural dynamics in native and denatured alpha‐lactalbumin
    Bu, Z; Cook, J; Callaway, DJ
  • Psychrophilic enzymes: revisiting the thermodynamic parameters of activation may explain local flexibility
    Lonhienne, T; Gerday, C; Feller, G
  • Picosecond dynamical changes on denaturation of yeast phosphoglycerate kinase revealed by quasielastic neutron scattering
    Receveur, V; Calmettes, P; Smith, JC; Desmadril, M; Coddens, G; Durand, D
  • Proteome analysis in the study of heat‐shock response
    Rosen, R; Ron, EZ

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