Allosteric Transitions

T to R transition of E. coli aspartate transcarbamoylase (Quicktime) (RealPlayer)

T to R transition of pig kidney fructose 1,6 bisphosphatase (Quicktime) (RealPlayer)

Catalytic Mechanisms

The catalytic mechanism of E. coli alkaline phosphatase (Quicktime) (RealPlayer)

The conformational changes associated with the ordered binding of carbamoyl phosphate and aspartate to E. coli aspartate transcarbamoylase (shown as a molecular surface). 50's loop is in blue, 80's loop in green and 240's loop in red. (RealPlayer) (QuickTime).

The conformational changes associated with the ordered binding of carbamoyl phosphate and aspartate to E. coli aspartate transcarbamoylase (shown as cartoon with selected side chains). 50's loop is in blue, 80's loop in green and 240's loop in red. (RealPlayer) (QuickTime)