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Dissociation of tetrameric ions of noncovalent streptavidin complexes formed by electrospray ionization
135
Citations
35
References
1995
Year
EngineeringBiological Mass SpectrometryTetrameric IonsChemistrySpectrochemical AnalysisIon ProcessAnalytical ChemistryNoncovalent Streptavidin ComplexesChromatographyBiochemistryPhysical ChemistryMass SpectraGas PhaseNatural SciencesCoordination ComplexMass SpectrometryProtein Mass SpectrometryElectrospray IonizationNative Mass SpectrometryMolecular ComplexMolecular FragmentationIon Structure
The noncovalent tetrameric association of the protein streptavidin formed by electrospray ionization (ESI) mass spectrometry has been observed intact and dissociated in the gas phase. An extended mass-to-charge ratio range quadrupole mass spectrometer was employed to examine the effects of harsher conditions in the ESI atmosphere-vacuum interface region on the streptavidin tetramer. Thermally induced dissociation caused the mass spectra to exhibit a series of complementary monomer and trimer ions that correspond to decomposition of the tetrameric species. Similar results were obtained with tandem mass spectrometric experiments on a Fourier transform ion cyclotron resonance mass spectrometer by application of sustained off-resonance irradiation (SORI) on a selected tetrameric charge state. The technique of single-frequency quadrupole excitation was used to accomplish selected-ion accumulation of the 14 + charge state of the tetramer during ion injection. Subsequent low energy SORI combined with broadband quadrupole cooling produced the 7 + monomer and 7 + trimer species, as well as the 6 + monomer and 8 + trimer complementary ions. The observed asymmetric breakup of the tetramer is qualitatively explained by using physical models.
| Year | Citations | |
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1991 | 644 | |
1991 | 496 | |
1991 | 462 | |
1991 | 324 | |
1990 | 323 | |
1993 | 291 | |
1994 | 261 | |
1990 | 244 | |
1988 | 238 | |
Site-directed mutagenesis studies of the high-affinity streptavidin-biotin complex: contributions of tryptophan residues 79, 108, and 120. Ashutosh Chilkoti, Ping-Heng Tan, Patrick S. Stayton Proceedings of the National Academy of Sciences Protein ChemistryProtein FunctionTryptophan Residues 79BiochemistryProtein Assembly | 1995 | 200 |
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