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The structure of the lectin and epidermal growth factor-related domains of E-selectin, an adhesion molecule involved with inflammation, provide further insight into selectin-carbohydrate interactions.
The rate of refolding of cytochrome c is very rapid in the absence of non-native interactions , which raises questions about the general significance of both the rates and intermediates of protein folding that are normally observed.
The structure of bi-functional thymidylate synthase-dihydrofolate reductase suggests that substrate may be channelled accross the surface of the protein between the two active sites.
Hhal methyltransferase, caught in the act of methylating a cytosine on a DNA substrate, reveals how the enzyme overcomes the problem of chemically modifying bases in the relatively inaccessible environment of the DNA duplex.
