FEBS Letters | |
Conformational effects of nucleotide exchange in ras p21 proteins as studied by fluorescence spectroscopy | |
Neidle, Stephen3  Kuroda, Reiko3  Drake, Alex1  Suter, David A.3  Hancock, John F.2  Skelly, Jane V.3  | |
[1] Department of Chemistry, Birkbeck College, 20, Gordon Street, London WC1H OQB, England;Academic Department of Haematology, Royal Free Hospital, London NW3 2QG, England;CRC Biomolecular Structure Unit, Institute of Cancer Research, Sutton, Surrey SM2 5NG, England | |
关键词: p21 ras protein; Guanine nucleotide binding; Tryptophan fluorescence; | |
DOI : 10.1016/0014-5793(90)80170-N | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
The intrinsic fluorescence properties of the oncogene protein p21N-ras, p21H-ras and one of its transforming mutants, p21N-ras (Va1112), have been investigated. A mutant containing a single tryptophan at position 28 in p21H-ras (Trp28) has been specifically engineered to provide a probe of protein conformation on nucleotide binding. The proteins produced essentially similar circular dichroism spectra typical of alpha/beta proteins. A decrease in the intensity of the fluorescence emission spectrum due to tyrosine occurred on GDP/GTP nucleotide exchange in the native and mutant proteins. Selective excitation of the single tryptophan in p21 produced a decrease in fluorescence intensity which was accompanied by a blue shift in the wavelength of maximum emission on nucleotide exchange. A reduction in the residual Mg2+ ion concentration enhanced this effect.
【 授权许可】
Unknown
【 预 览 】
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