Infrared spectroscopy of single-turn and double-turn tethered alpha-helices in the gas phase: don't let your left hand know what your right hand is doing.
Zwier, Timothy S.
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https://hdl.handle.net/2142/107322
Description
Title
Infrared spectroscopy of single-turn and double-turn tethered alpha-helices in the gas phase: don't let your left hand know what your right hand is doing.
Author(s)
Zwier, Timothy S.
Contributor(s)
Lawler, John T.
Issue Date
2020-06-24
Keyword(s)
Conformers and isomers
Abstract
This talk will describe single-conformation IR and UV spectroscopy of a series of single-turn and double-turn alpha helices as cryo-cooled, gas phase ions. Synthesized samples of tethered pentapeptides are known to form single-turn alpha helices in aqueous solution. When L-amino acids are used, a right-handed single-turn helix is formed while D-amino acids produce a left-handed helix. Due to the tether, these structures are remarkably stable in aqueous solution over a wide range of temperatures, pH, and denaturant. They can be concatenated, making LL, DD, LD, and DL double-turn forms. When a methylated arginine is placed at the C-terminal end of the tethered peptide, single-turn helices are the most stable structure, and are observed exclusively. The spectra in the NH stretch and amide I regions show distinct effects that depend on position along the helix, and the presence or absence of a kink due to concatenation of two opposite-handed helices. We will discuss these spectra and the prospects they offer as scaffolds for studying a wide range of interesting structural and dynamical problems.
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