期刊
FARADAY DISCUSSIONS
卷 150, 期 -, 页码 209-226出版社
ROYAL SOC CHEMISTRY
DOI: 10.1039/c1fd00001b
关键词
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资金
- National Science Foundation [NSF-CHE0909619, CHE-0848847]
- German Academic Exchange Service (DAAD)
Single-conformation ultraviolet and infrared spectra of a series of model gamma-peptides are reported, with the goal of providing new tests of amide stacking as an amide-amide binding motif. The data also serve to illustrate the power and challenges of carrying out single-conformation spectroscopy of neutral molecules of this size in the gas phase under jet-cooled conditions. Building on recent work on Ac-gamma(2)-hPhe-NHMe (James et al., J. Am. Chem. Soc., 2009, 131, 14243), the effects of derivatization and H2O complexation on amide stacking are studied. Ac-gamma(2)-hPhe-N(Me)(2) shows only amide stacked structures, blocking the competing position for formation of an amide-amide H-bond. The Ac-gamma(2)-hPhe-NHMe-H2O complex includes structures in which the H2O molecule forms a bridge between the two stacked amide planes, retaining and enhancing amide stacking. IR population transfer methods are also employed to study the dynamics of photodissociation of the amide stacked-H2O complex. Finally, IR ion-gain spectroscopy is introduced as a means of recording infrared spectra containing contributions from all conformers present, based on IR-induced broadening of the UV absorptions. Its role in estimating fractional abundances is tested on Ac-gamma(2)-hPhe-NHMe.
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