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H-Bonding in a Progressively Solvated Macrocyclic Peptide.

© 2012 EPFL

26.04.12 - Interplay of Intra- and Intermolecular H-Bonding in a Progressively Solvated Macrocyclic Peptide.

Studying solvation of a large molecule on an atomic level is challenging because of the transient character and inhomogeneity of hydrogen bonding in liquid water. The group of MER Oleg Boyarkine(Laboratory of Molecular Physical Chemistry) studied water clusters of a protonated macrocyclic decapeptide, gramicidin S, which were prepared in the gas phase and then cooled to cryogenic temperatures. The experiment spectroscopically tracked fine structural changes of the clusters upon increasing the number of attached water molecules from 1 to 50 and distinguished vibrational fingerprints of different conformers. The data indicate that only the first two water molecules induce a substantial change of the gramicidin S structure by breaking two intramolecular noncovalent bonds. The peptide structure remains largely intact upon further solvation, reflecting the interplay between the strong intramolecular and weaker intermolecular hydrogen bonds.

Natalia S. Nagornova, Thomas R. Rizzo, Oleg V. Boyarkine, Science 20 April 2012: Vol. 336 no. 6079 pp. 320-323 DOI: 10.1126/science.1218709 (2012)

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Olivier Glauser
Master en Informatique et systèmes de communication 1994
1994 - 1996 HP
1996 - 1998 Phillippe Moris
1998 - 2005 MBA Universite de Harvard
2005 - 2009 ROTH Cl Partners
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