ISSN:
1435-1536
Keywords:
13C NMR CP/MAS spectroscopy
;
secondary structure keratins
;
cytochrome C
;
myoglobin
Source:
Springer Online Journal Archives 1860-2000
Topics:
Chemistry and Pharmacology
,
Mechanical Engineering, Materials Science, Production Engineering, Mining and Metallurgy, Traffic Engineering, Precision Mechanics
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF01452215
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