Low‐sulfur proteins from α‐keratins. Interrelationships between their amino acid compositions, α‐helix contents, and the supercontraction of the parent keratin
- 1 September 1966
- journal article
- research article
- Published by Wiley in Biopolymers
- Vol. 4 (8), 905-916
- https://doi.org/10.1002/bip.1966.360040807
Abstract
No abstract availableThis publication has 42 references indexed in Scilit:
- Sequential polypeptides containing S-benzyl-l-cysteinyl and γ-ethyl-l-glutamyl residuesJournal of Molecular Biology, 1965
- Structure and function of haemoglobinJournal of Molecular Biology, 1965
- Sequential polypeptides containing L-valyl and γ-methyl-L-glutamyl residuesJournal of Molecular Biology, 1965
- Synthesis and conformation of a copolymer of ε-carbobenzoxy-l-lysine and S-carbobenzoxy-l-lysineBiochimica et Biophysica Acta (BBA) - Specialized Section on Biophysical Subjects, 1964
- Studies on Synthetic Polypeptide Antigens. VI. The Synthesis and Physical Chemical Properties of a New Group of Linear-chain AntigensJournal of the American Chemical Society, 1962
- The fine structure of α-keratinJournal of Molecular Biology, 1961
- The relation between the disulphide content of wool and the two-stage supercontraction of wool fibres in solutions of LiBrBiochimica et Biophysica Acta, 1961
- THE DEPENDENCE OF THE CONFORMATIONS OF SYNTHETIC POLYPEPTIDES ON AMINO ACID COMPOSITION1,2Journal of the American Chemical Society, 1960
- Structural features of keratin suggested by its mechanical propertiesBiochimica et Biophysica Acta, 1959
- X-Ray studies of the structure of hair, wool, and related fibres. II.- the molecular structure and elastic properties of hair keratinPhilosophical Transactions of the Royal Society A, 1933