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Issue 16, 2003
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Structural changes in the Ras protein revealed by fluorescence spectroscopy

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The Y32W mutant of the Ras protein which has a tryptophan residue close to the guanine nucleotide binding site is studied using two fluorescence spectroscopic techniques. Two-dimensional mapping of all emission and all fluorescence spectra using excitation–emission spectroscopy (EES) in conjunction with time-resolved laser-induced fluorescence (LIF) is used to analyze and assign the contribution of the different fluorophores to the total fluorescence. Time-resolved LIF is shown to be a method that allows to follow the slight conformational changes of Ras binding to the nucleotides GDP, GTP, or the non-hydrolyzable analogues GppNHp, GppCH2p and GTP-γS and allows to distinguish between the active and inactive form. Additionally, a variant of the EES technique is used for the investigation of the intrinsic GTPase function of Ras and the determination of kinetic constants for this reaction.

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Publication details

The article was received on 25 Mar 2003, accepted on 19 Jun 2003 and first published on 09 Jul 2003

Article type: Paper
DOI: 10.1039/B303262K
Citation: Phys. Chem. Chem. Phys., 2003,5, 3498-3506
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    Structural changes in the Ras protein revealed by fluorescence spectroscopy

    A. Brockhinke, R. Plessow, K. Kohse-Höinghaus and C. Herrmann, Phys. Chem. Chem. Phys., 2003, 5, 3498
    DOI: 10.1039/B303262K

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