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Energy of Hydrogen Bonds Probed by the Adhesion of Functionalized Lipid Layers

Abstract : It is now well admitted that hydrophobic interactions and hydrogen bonds are the main forces driving protein folding and stability. However, because of the complex structure of a protein, it is still difficult to separate the different energetic contributions and have a reliable estimate of the hydrogen bond part. This energy can be quantified on simpler systems such as surfaces bearing hydrogen-bonding groups. Using the surface force apparatus, we have directly measured the interaction energy between monolayers of lipids whose headgroups can establish hydrogen bonds in water: nitrilotriac-etate, adenosine, thymidine, and methylated thymidine lipids. From the adhesion energy between the surfaces, we have deduced the energy of a single hydrogen bond in water. We found in each case an energy of 0.5 kcal/mol. This result is in good agreement with recent experimental and theoretical studies made on protein systems showing that intramolecular hydrogen bonds make a positive contribution to protein stabilization.
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David Tareste, Frédéric Pincet, Eric Perez, Stéphane Rickling, Charles Mioskowski, et al.. Energy of Hydrogen Bonds Probed by the Adhesion of Functionalized Lipid Layers. Biophysical Journal, Biophysical Society, 2002, ⟨10.1016/S0006-3495(02)75367-8⟩. ⟨inserm-02296710⟩



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