Thermodynamics Research - Enthalpy, Entropy, Energy Transitions

Thermodynamics Research Today is a free monthly online journal that collates and summarizes the latest research about Thermodynamics, including details on enthalpy, entropy, energy transitions.


Thermodynamics Research Today

Home

View Latest Issue

Information About Thermodynamics

Books on Thermodynamics

Advertising in Research Today

View Other Research Today Publications



The conformational stability and thermodynamics of Fur A (ferric uptake regulator) from Anabaena sp. PCC 7119.

Hernández JA, Meier J, Barrera FN, de los Paños OR, Hurtado-Gómez E, Bes MT, Fillat MF, Peleato ML, Cavasotto CN, Neira JL

Departamento de Bioquímica y Biología Molecular y Celular, Universidad de Zaragoza, Zaragoza, Spain.

Fur (ferric uptake regulator) is a key bacterial protein that regulates iron acquisition and its storage, and modulates the expression of genes involved in the response to different environmental stresses. Although the protein is involved in several regulation mechanisms, and members of the Fur family have been identified in pathogen organisms, the stability and thermodynamic characterization of a Fur protein have not been described. In this work, the stability, thermodynamics and structure of the functional dimeric Fur A from Anabaena sp. PCC 7119 were studied by using computational methods and different biophysical techniques, namely, circular dichroism, fluorescence, Fourier-transform infrared, and nuclear magnetic resonance spectroscopies. The structure, as monitored by circular dichroism and Fourier-transform infrared, was composed of a 40% of alpha-helix. Chemical-denaturation experiments indicated that Fur A folded via a two-state mechanism, but its conformational stability was small with a value of DeltaG = 5.3 +/- 0.3 kcal mol(-1) at 298 K. Conversely, Fur A was thermally a highly stable protein. The high melting temperature (Tm = 352 +/- 5 K), despite its moderate conformational stability, can be ascribed to its low heat capacity change upon unfolding, DeltaCp, which had a value of 0.8 +/- 0.1 kcal mol(-1) K(-1). This small value is probably due to burial of polar residues in the Fur A structure. This feature can be used for the design of mutants of Fur A with impaired DNA-binding properties.

Published 1 December 2005 in Biophys J, 89(6): 4188-200.
Full-text of this article is available online (may require subscription).

Place a permanent text-link or advertisement here for just US$15.

© 2005-2008 Thermodynamics Research Today. All Rights Reserved.



Thermodynamics Research Today Archive:

Volume 1 (2005)
  Issue 1 (August)
  Issue 2 (September)
  Issue 3 (October)
  Issue 4 (November)
  Issue 5 (December)

Volume 2 (2006)
  Issue 1 (January)
  Issue 2 (February)
  Issue 3 (March)
  Issue 4 (April)
  Issue 5 (May)
  Issue 6 (June)
  Issue 7 (July)
  Issue 8 (August)
  Issue 9 (September)
  Issue 10 (October)
  Issue 11 (November)
  Issue 12 (December)

Volume 3 (2007)
  Issue 1 (January)
  Issue 2 (February)
  Issue 3 (March)
  Issue 4 (April)
  Issue 5 (May)
  Issue 6 (June)
  Issue 7 (July)
  Issue 8 (August)
  Issue 9 (September)
  Issue 10 (October)
  Issue 11 (November)
  Issue 12 (December)

Volume 4 (2008)
  Issue 1 (January)
  Issue 2 (February)
  Issue 3 (March)
  Issue 4 (April)
  Issue 5 (May)
  Issue 6 (June)
  Issue 7 (July)
  Issue 8 (August)
  Issue 9 (September)
  Issue 10 (October)



Thermodynamics Books

Problems and Solutions on Thermodynamics and Statistical Mechanics (Major American Universities Ph.D. Qualifying Questions and Solutions)

Problems and Solutions on Thermodynamics and Statistical Mechanics (Major American Universities Ph.D. Qualifying Questions and Solutions)