N‐Alkylacylamides in Thin Films Display Infrared Spectra of 310‐, α‐, and π‐Helices with Visible Static and Dynamic Growth Phases |
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| Authors: | Prof. Edward M. Kosower Galina Borz |
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| Affiliation: | School of Chemistry, Tel‐Aviv University, Ramat‐Aviv, Tel‐Aviv 69978 (Israel) |
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| Abstract: | A peptide model is a physical system containing a CONH group, the simplest being HCONHCH3, N‐methylformamide (NMF). We have discovered that NMF and N‐methylacetamide (NMA), which form hydrogen‐bonded oligomers in thin films on a planar AgX fiber, display infrared (IR) spectra with peaks like those of polypeptide helices. Structures can be assigned by their amide I maxima near 1672 (310), 1655 (310), 1653 (α), 1655 (π), and 1635 cm?1 (π), which are the first IR data for the π‐helix. Sharp peaks are an outcome of immobilization of polar species on the polar surface of silver halides. We report the first use of expanded thin‐film IR spectroscopy, in which plots of every spectrum over the amide I–II range show pauses or slow stages in the increase or decrease of absorption. These are identified as static phases followed by dynamic phases, with the incremental gain or loss of a helix turn. A general theory can be stated for such processes. Density functional calculations show that the NMA α‐helix pentamer (crystal structure geometry) is transformed into a π‐helix‐like form. For the first time, an entire sequence (310‐helix, α‐helix, π‐helix, quasiplanar species) of spectra has been recorded for NMA. |
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| Keywords: | helical structures hydrogen‐bonded peptides IR spectroscopy N‐alkylacylamides planar fibers |
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