Alternating Current Bridge Methods 6th ed by B. Hague

By B. Hague

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Nature, 432, 925, 2004. ) groups to cocrystallize the wild-type toxin with a substrate bound in the active site. The single point mutation E224Q impairs substrate turnover,19 but a second mutation Y366F was required to completely abolish all substrate turnover at the high protein/substrate concentrations required for crystallization studies. 1 Residues 141–204 of SNAP-25 were then cocrystallized with the inactive double mutant of BoNT/A-LC and the peptide was found to interact extensively with the toxin, with 4,840 Å2 of buried surface area.

Struct. , 4, 788, 1997. 4. B. , Unraveling the structures and modes of action of bacterial toxins, Curr. Opin. Struct. , 8, 778, 1998. 5. Eswaramoorthy, S. , Role of metals in the biological activity of Clostridium botulinum neurotoxins, Biochemistry, 43, 2209, 2004. 6. , Neurotoxins affecting neuroexocytosis. Physiol. , 80, 717, 2000. 7. Schiavo, G. , 335, 99, 1993. 8. Binz T. , Proteolysis of SNAP-25 by types E and A botulinum neurotoxins. J. Biol. , 269, 1617, 1994. fm Page 44 Sunday, September 24, 2006 10:02 AM 44 Treatments from Toxins 9.

4) — two in VAMP, and two in syntaxin. It was proposed that the neurotoxin recognizes at least one of these motifs in addition to the region spanning the scissile bond. Deletion mutation studies have been carried out on SNAP-25 to identify the optimum length required for proteolytic cleavage by BoNT/E. SNAP-25 (93–206) was cleaved as efficiently as the full-length SNAP-25 (1–206); so was SNAP-25 (146–206). However, the effect of BoNT/A was drastically reduced with SNAP-25 (156–206), although less so for BoNT/E.

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