X-ray studies of the distribution of protein chain types in the vertebrate epidermis
References (28)
Ergeb. d. Biol.
(1926)Zeits. f. Zellforsch. u. mikros. Anat.
(1926)- et al.
Phil. Trans. Roy. Soc., A
(1933)J.C.S.
(1942)Nature
(1943) - et al.
Biochimica et Biophysica Acta
(1947) Anat. Hefte
(1909)Q.J.M.S.
(1882)Zeits. f. Zellforsch. u. mikros. Anat.
(1926)J. Biol. Chem.
(1941)- et al.
J. Text. Sci. Leeds
Ergeb. d. Biol.
Morph. Jahrb.
Aquila
Cited by (74)
Molecular structure of sauropsid β-keratins from tuatara (Sphenodon punctatus)
2019, Journal of Structural BiologyCitation Excerpt :In addition to the β-keratins (Fraser et al., 1972), also referred to as the corneous β-proteins (CBPs; Holthaus et al., 2019), both intermediate filaments (IF) and corneous proteins of the Epidermal Differentiation Complex (EDC: Rice et al., 2013; Strasser et al., 2015; Wu et al., 2015) form the epidermal appendages of birds and crocodiles (the archosaurs), turtles (the testudines), lizards and snakes (the squamates - a branch of the lepidosaurs) and tuatara (the rhynchocephalia – also a branch of the lepidosaurs) (Fig. 1). Characteristic structural features of all of these proteins excluding those from tuatara have been identified from studies of their amino acid sequences (Fraser and MacRae, 1976, Fraser and Parry, 1996, 2008, 2011, 2014), from infrared spectroscopy (Fraser and Suzuki, 1965, Suzuki, 1973) and from X-ray diffraction analyses (Astbury and Marwick, 1932, Rudall, 1947, Bear and Rugo, 1951, Fraser and MacRae, 1959, 1963, Schorr and Krimm, 1961). In particular, the presence of a highly-conserved region of 34-residues has been recognized as having a high potential to form a twisted β-sheet (Fraser et al., 1971), believed to be right-handed, with one of the two faces consisting largely of apolar residues (Fraser and Parry, 2008, 2011, 2014).
Keratin: Structure, mechanical properties, occurrence in biological organisms, and efforts at bioinspiration
2016, Progress in Materials ScienceCitation Excerpt :Fig. 47c shows schematically the structural changes of α → β → α at different strains during load–unload cycle [116]. Feathers and avian and reptilian scales show the same keratin genes [228], and it is well-accepted that the hard keratin of feathers and these scales is the β-sheet based on X-ray diffraction patterns [24,26,57,100,229,230] and transmission electron microscopy [16,91]. Therefore, feathers are discussed here representing both.
The Process of Cornification Evolved From the Initial Keratinization in the Epidermis and Epidermal Derivatives of Vertebrates: A New Synthesis and the Case of Sauropsids
2016, International Review of Cell and Molecular BiologySkin lipid structure controls water permeability in snake molts
2014, Journal of Structural BiologyUltrastructural immunolocalization of alpha-keratins and associated beta-proteins (beta-keratins) suggests a new interpretation on the process of hard and soft cornification in turtle epidermis
2013, MicronCitation Excerpt :The contribution of alpha-keratins and beta-proteins in the formation of corneous layers of different resistance in turtle epidermis is little understood. The presence of a soft epidermis in the soft-shelled turtles was correlated to the absence of beta-keratin in these species (Rudall, 1947; Baden and Maderson, 1970). Immunoblotting and immunocytochemical studies however indicated that small amount of beta-proteins, perhaps lacking the central beta-pleated region, were present in the soft epidermis of turtles (Alibardi et al., 2004; Alibardi and Toni, 2005, 2006).