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Article Dans Une Revue ChemPhysChem Année : 2011

Compact Folding of Isolated Four-Residue Neutral Peptide Chains: H-Bonding Patterns and Entropy Effects

Eric Gloaguen

Résumé

The intrinsic folding of isolated neutral tetrapeptides is investigated by IR-UV double-resonance laser spectroscopy coupled to quantum chemistry (DFT-D) calculations. Laser-desorbed jet-cooled Ac-(Ala)(3)-Phe-NH(2) as well as two other related four-residue molecules are shown to fold according to the same 14-7L-X-10II'-7L compact, beta-hairpin-like backbone pattern, leading to a remarkable closed daisy chain of H-bonds along the molecule. Thermodynamic calculations confronted to the abundances observed show that these laser-desorbed peptides are best described by a finite conformational temperature (typically ca. 300-450 K), which suggests that not only enthalpy but also entropy effects play an important role in selecting these structures within this temperature range.

Dates et versions

hal-00656143 , version 1 (03-01-2012)

Identifiants

Citer

R.-J. Plowright, Eric Gloaguen, M. Mons. Compact Folding of Isolated Four-Residue Neutral Peptide Chains: H-Bonding Patterns and Entropy Effects. ChemPhysChem, 2011, 12 (10), pp.1889-1899. ⟨10.1002/cphc.201001023⟩. ⟨hal-00656143⟩
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