期刊
CHEMPHYSCHEM
卷 12, 期 10, 页码 1889-1899出版社
WILEY-BLACKWELL
DOI: 10.1002/cphc.201001023
关键词
density functional calculations; hydrogen bonds; IR spectroscopy; peptides; UV spectroscopy
资金
- Agence Nationale de la Recherche [ANR-08-BLAN-0158-01]
- Agence Nationale de la Recherche (ANR) [ANR-08-BLAN-0158] Funding Source: Agence Nationale de la Recherche (ANR)
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.
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