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Fluorescence approaches to the study of the p21ras GTPase mechanism
J F Eccleston1, K J Moore, G G Brownbridge
1Division of Physical Biochemistry, National Institute for Medical Research, Mill Hill, London, U.K.
Biochemical Society Transactions
|April 1, 1991
Abstract:
The use of ribose-modified guanine nucleotides and tryptophan mutants of p21ras, neither of which have significant effect on the kinetic mechanism of the p21ras GTPase and the GAP-activated p21ras GTPase, will now allow a detailed kinetic study of how GAP and other regulatory proteins interact with p21ras. This will lead to a better understanding of how the relative concentrations of 'active' p21ras. GTP and 'inactive' p21ras. GDP are regulated in the cell.