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pro vyhledávání: '"Amy Westcott"'
Autor:
Celia Bonaventura, Amy Westcott, Gregory Cole, Danielle Mercatante, Shirley Tesh, Richard W. Topham, Greer Kaufman
Publikováno v:
Archives of biochemistry and biophysics. 369(2)
The copper-containing hemocyanins are a class of oxygen-transport proteins whose structures differ in arthropods and molluscs. Crystal structure analyses and amino acid sequence comparisons show that disulfide bonding is a common feature in both arth
Autor:
Richard W. Topham, Celia Bonaventura, Amy Westcott, Gregory Cole, Shirley Tesh, Danielle Mercatante
Publikováno v:
Archives of biochemistry and biophysics. 352(1)
The crystal structure analysis of Subunit II of Limulus hemocyanin has shown that its polypeptide chain is folded into three distinct structural domains. The oxygen-binding, dinuclear copper center is located deep in the core of Domain 2. Two disulfi