Protein carbohydrate thermodynamics 1/887- conformation

New glycolipids have to be synthesized to get further insights into liquid crystal properties (mainly lyotropic liquid crystals), surfactant properties (useful in the extraction of membrane proteins), and factors that govern vesicle formation, stability and tightness. New techniques have to be perfected in order to allow to make precise measurements of thermodynamic and kinetic parameters of binding in 3D-systems and to refine those already avalaible with 2D-arrays. Furthermore, molecular mechanics calculations should also be improved to afford a better modeling of the conformations of carbohydrates at interfaces, in relation with physical measurements such as NMR. 

The decrease in entropy that is usually observed in carbohydrate-protein interactions could partly be due to the restriction of conformational mobility of the substrate on complex formation. Also, effects of complex formation on the conformational changes in the protein should affect the overall thermodynamics of binding. Reinforcement of interactions that stabilize the overall protein conformation during substrate binding can contribute to the exothermicity of the reaction, for example, while rigidification of the peptide chain or reduction of the mobility of the functional groups inside the active center should have an adverse effect on entropy. 

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