May 26, 2012

Thermodynamic impact of embedded water molecules in the unfolding of human CD2BP2-GYF domain

The Journal of Physical Chemistry. B
Montserrat Andujar-SanchezJose C Martinez


GYF domains are small polyproline-recognition modules adopting a structural arrangement consisting of a single α-helix packed against a small β-sheet. Although most families of proline-rich recognition modules have been extensively characterized in terms of function, structure, or conformational flexibility, little is known about GYF domain functionality and folding. We have undertaken the thermodynamic characterization of the unfolding of CD2BP2-GYF domain by combining differential scanning calorimetry and circular dichroism under different pH conditions. The experimental data can be well-described in terms of a two-state equilibrium, although an unusually high heat capacity of the native state reflects a considerable conformational flexibility and dynamics of CD2BP2-GYF domain. In addition, the normalized thermodynamic parameters of unfolding (enthalpy, entropy and heat capacity) are roughly a factor of two greater than expected. In contrast, stability curves reveal an ordinary unfolding behavior of CD2BP2-GYF domain in terms of Gibbs energies, incurring thus unusually strong enthalpy-entropy compensation. This phenomenon, previously described as "thermodynamic homeostasis", has been associated in different examples to the co...Continue Reading

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Mentioned in this Paper

Molecular Helix
CD2 Antigens
Tertiary Protein Structure
Helix (Snails)
Body Cavities
Dental Caries
Calorimetry, Differential Scanning

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