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Energy of hydrogen bonds probed by the adhesion of functionalized lipid layers
David Tareste1, Frédéric Pincet, Eric Perez
1Laboratoire de Physique Statistique de l'Ecole Normale Supérieure, Unité de Recherche Associée Centre National de la Recherche Scientifique, 1306 Associée aux Universités Paris VI et Paris VII, 24 rue Lhomond, 75231 Paris cedex 05, France.
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: nitrilotriacetate, 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.