A study of conformational stability of polypeptide blends by solid state two-dimensional 13C–1H heteronuclear correlation NMR spectroscopy
| Autor: | Shigeki Kuroki, Katsuyoshi Murata, Hiroyuki Kono, Isao Ando, Etsuko Katoh |
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| Rok vydání: | 2003 |
| Předmět: |
Polymers and Plastics
Hydrogen bond Chemistry Organic Chemistry Intermolecular force Nuclear magnetic resonance spectroscopy Miscibility Crystallography chemistry.chemical_compound Solid-state nuclear magnetic resonance Heteronuclear molecule Polymer chemistry Materials Chemistry Trifluoroacetic acid Polymer blend |
| Zdroj: | Polymer. 44:4021-4027 |
| ISSN: | 0032-3861 |
| Popis: | The intermolecular hydrogen-bond interactions in polyglycine (PG)/poly(L-valine) (PLV) blend with a ratio of 1/1 have been studied through high-speed frequency-switched Lee – Goldburg (FSLG) 13 C– 1 H heteronuclear correlation (HETCOR) NMR experiments, where the PG/PLV blend sample is prepared by adding trifluoroacetic acid (TFA) solution of their polypeptide mixture containing a 2.0 wt/wt% amount of sulfuric acid (H2SO4) to alkaline water. The spectral assignment of the polypeptide blend is made by using multiple proton cross-peaks, which appeared in the HETCOR spectra. Intermolecular correlation peaks between PG(b-sheet) and PLV(b-sheet) appear in the HETCOR spectra with long contact time. From these experimental results, it has been clarified that intermolecular hydrogen-bond interactions ðsCyO ··· H – NrÞ between the PG(b-sheet) and PLV(b-sheet) are formed and thus the PG/PLV blend with high miscibility is formed. q 2003 Elsevier Science Ltd. All rights reserved. |
| Databáze: | OpenAIRE |
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