Abstract
Low angle X-ray diffraction is a powerful means of investigating long range axial order in fibrous protein structures, and α-keratin was one of the earliest materials to be studied by this method1. The observed meridional and near-meridional reflexions have been indexed2–5 as orders of an axial period of 198 Å, but there are indications6,7 that this might not be correct. This possibility has been investigated using a high resolution focusing X-ray camera8 to obtain diffraction patterns from several native keratins and from certain heavyatom derivatives of porcupine quill.
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FRASER, R., MACRAE, T. Structure of α-Keratin. Nature 233, 138–140 (1971). https://doi.org/10.1038/233138a0
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DOI: https://doi.org/10.1038/233138a0
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