ANSTO Publications Online >
Journal Publications >
Journal Articles >
Please use this identifier to cite or link to this item:
|Title: ||Thermal fluctuations of haemoglobin from different species: adaptation to temperature via conformational dynamics|
|Authors: ||Stadler, AM|
|Keywords: ||BODY TEMPERATURE|
|Issue Date: ||7-Nov-2012|
|Publisher: ||THE ROYAL SOCIETY|
|Citation: ||Stadler, A. M., Garvey, C. J., Bocahut, A., Sacquin-Mora, S., Digel, I., Schneider, G. J., Natali, F., Artmann, G. M., & Zaccai, G. (2012). Thermal fluctuations of haemoglobin from different species: adaptation to temperature via conformational dynamics. Journal of the Royal Society Interface, 9(76), 2845-2855.|
|Abstract: ||Thermodynamic stability, configurational motions and internal forces of haemoglobin (Hb) of three endotherms (platypus, Ornithorhynchus anatinus; domestic chicken, Gallus gallus domesticus and human, Homo sapiens) and an ectotherm (salt water crocodile, Crocodylus porosus) were investigated using circular dichroism, incoherent elastic neutron scattering and coarse-grained Brownian dynamics simulations. The experimental results from Hb solutions revealed a direct correlation between protein resilience, melting temperature and average body temperature of the different species on the 0.1 ns time scale. Molecular forces appeared to be adapted to permit conformational fluctuations with a root mean square displacement close to 1.2 Å at the corresponding average body temperature of the endotherms. Strong forces within crocodile Hb maintain the amplitudes of motion within a narrow limit over the entire temperature range in which the animal lives. In fully hydrated powder samples of human and chicken, Hb mean square displacements and effective force constants on the 1 ns time scale showed no differences over the whole temperature range from 10 to 300 K, in contrast to the solution case. A complementary result of the study, therefore, is that one hydration layer is not sufficient to activate all conformational fluctuations of Hb in the pico- to nanosecond time scale which might be relevant for biological function. Coarse-grained Brownian dynamics simulations permitted to explore residue-specific effects. They indicated that temperature sensing of human and chicken Hb occurs mainly at residues lining internal cavities in the β-subunits. Copyright © The Royal Society 2012.|
|Appears in Collections:||Journal Articles|
Files in This Item:
There are no files associated with this item.
Items in APO are protected by copyright, with all rights reserved, unless otherwise indicated.