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Secondary structure of peptides 16th. Characterization of proteins by means of13C NMR CP/MAS spectroscopy

  • Polymer Science
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Abstract

50.3 or 75.4 MHz13C NMR cross-polarization/magic angle spinning spectra of human hair, horse hair, horse hoof, parrot feather, sperm whale myoglobin, and horse heart cytochrome C were measured. The spectra of human hair and horse hair indicate nearly equal mole fractions ofΒ-sheets andα-helices and a low percentage of amorphous regions, whereas horse hoof contains a higher fraction of amorphous proteins. The parrot feathers contain a smallα-helix fraction (ca. 10±5 %) in additon to a largeΒ-sheet fraction whereas cytochrome C contains 70–90%α-helices. The spectrum of myoglobin could not interpreted in terms of defined secondary structures. The usefulness of the13C NMR CP/MAS spectroscopy for the characterization of proteins is compared with that of IR spectroscopy and X-ray diffraction.

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Author notes

  1. H. R. Kricheldorf

    Present address: Institut für Angewandte Chemie der UniversitÄt Hamburg, Hamburg, FRG

Authors and Affiliations

  1. Institut für Angewandte Chemie der UniversitÄt Hamburg, Hamburg, FRG

    D. Müller

  2. Bruker Analytische Me\technik, Rheinstetten, FRG

    H. R. Kricheldorf & D. Müller

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  1. H. R. Kricheldorf
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  2. D. Müller
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Kricheldorf, H.R., Müller, D. Secondary structure of peptides 16th. Characterization of proteins by means of13C NMR CP/MAS spectroscopy. Colloid & Polymer Sci 262, 856–861 (1984). https://doi.org/10.1007/BF01452215

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  • DOI: https://doi.org/10.1007/BF01452215

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