title: Fluorescence approaches to the study of the p21ras GTPase mechanism.
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.
authors.affiliation: Division of Physical Biochemistry, National Institute for Medical Research, Mill Hill, London, U.K.
authors.forename: J F
authors.initials: JF
authors.lastname: Eccleston
authors.forename: K J
authors.initials: KJ
authors.lastname: Moore
authors.forename: G G
authors.initials: GG
authors.lastname: Brownbridge
authors.forename: M R
authors.initials: MR
authors.lastname: Webb
authors.forename: P N
authors.initials: PN
authors.lastname: Lowe
mesh_terms: D020558:GTP Phosphohydrolases / Q000378:metabolism*; D020690:GTPase-Activating Proteins; D007700:Kinetics; D016297:Mutagenesis, Site-Directed; D011506:Proteins / Q000378:metabolism*; D016283:Proto-Oncogene Proteins p21(ras) / Q000235:genetics / Q000378:metabolism*; D013050:Spectrometry, Fluorescence / Q000379:methods; D020703:ras GTPase-Activating Proteins
chemical_list: D020690:GTPase-Activating Proteins; D011506:Proteins; D020703:ras GTPase-Activating Proteins; D020558:GTP Phosphohydrolases; D016283:Proto-Oncogene Proteins p21(ras)