Structure of α-keratin: Structural implication of the amino acid sequences of the type I and type II chain segments

Autor:	R.D.B. Fraser, W.G. Crewther, T.P. MacRae, David A.D. Parry
Rok vydání:	1977
Předmět:	chemistry.chemical_classification Periodicity Protein Conformation Stereochemistry Ionic bonding Type (model theory) Amino acid Protein structure chemistry Chain (algebraic topology) Structural Biology Keratin Keratins Amino Acid Sequence Molecular Biology Peptide sequence
Zdroj:	Journal of Molecular Biology. 113:449-454
ISSN:	0022-2836
DOI:	10.1016/0022-2836(77)90153-x
Popis:	Two amino acid sequences from potentially helical fragments of low-sulphur proteins from α-keratin have been analysed computationally and periods 9.4 and 28 residues long noted in the axial disposition of charged residues. Ionic interactions between chains have also been calculated and these indicate a preference for the helical fragments to aggregate in parallel with zero shift between chains in a manner essentially identical to that found for α-tropomyosin.
Databáze:	OpenAIRE
Externí odkaz:	https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8b6a65054c6c1901eab8df16d6757a47 https://doi.org/10.1016/0022-2836(77)90153-x Zobrazit plný text záznamu