PMID: 11911899Mar 26, 2002Paper

The parallel helices of the intermediate filaments of alpha-keratin

International Journal of Biological Macromolecules
Max FeughelmanBarry Willis

Abstract

Recent Fourier transform infrared spectroscopy (FTIR) with attenuated total reflection technique (ATR) has been applied to alpha-keratin fibers (horse-hair) extended in water both at 21 and 95 degrees C. Infrared absorption bands in the Amide 1 region indicated that at extensions to 40-50% strain in water at 21 degrees C alpha-helices had completely disappeared and parallel beta-sheets were formed [Appl. Spectrosc. 55 (2001) 552]. However, when the hair fibers were extended to the same strain at 95 degrees C in water the result was the formation of anti-parallel beta-sheets. These results suggest that the relatively more stable anti-parallel beta-state [Polymer 10 (1969) 810] is only attained in extended alpha-keratin fibers at elevated temperatures and must result from major molecular rearrangement. It was concluded that the alpha-helices in the intermediate filaments (IFs) of alpha-keratin fibers must be parallel. This is in contrast to the previously accepted orientation of anti-parallel alpha-helices, based primarily on findings of X-ray diffraction studies of the structure of beta-keratin in highly extended fibers [Polymer 10 (1969) 810; Keratins, IL: Thomas Springfield (1972); Nature 316 (1985) 767].

References

Mar 2, 1986·Nature·M Feughelman
Aug 4, 1985·Nature·P M Steinert, A C Steven
Apr 15, 1972·Comparative Biochemistry and Physiology. B, Comparative Biochemistry·J M Gillespie
Oct 1, 1968·Biopolymers·M Feughelman, T W Mitchell

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Citations

Mar 8, 2013·International Journal of Biological Macromolecules·Annalisa AluigiMaurizio Canetti
May 9, 2009·Journal of Anatomy·Hermann H Bragulla, Dominique G Homberger

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