Disulphide bonding in α-keratin

Autor: L.G. Sparrow, R.D.B. Fraser, David A.D. Parry, T.P. MacRae
Rok vydání: 1988
Předmět:
Zdroj: International Journal of Biological Macromolecules. 10:106-112
ISSN: 0141-8130
DOI: 10.1016/0141-8130(88)90017-7
Popis: Epidermal appendages such as hair and nail contain a complex mixture of proteins known as α-keratin. Their chemical inertness, and many of their physical characteristics, are governed by the high content of disulphide linkages between the protein chains. Sufficient data on the amino acid sequences of the constituent proteins are now available to provide insights into the nature and distrubution of these linkages in the three-dimensional structure of the α-keratin complex. From stereochemical considerations constraints on the formation of disulphide linkages in and between two-strand coiled-coil ropes were identified. In earlier studies certain staggers between rod domain segments were shown to be favoured on the basis of ionic interactions and in the present studies one of these was also found to have a high potential for disulphide bond formation.
Databáze: OpenAIRE