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Science 13 April 1990:
Vol. 248. no. 4952, pp. 201 - 204
DOI: 10.1126/science.2326633

Articles

Science, Vol 248, Issue 4952, 201-204
Copyright © 1990 by American Association for the Advancement of Science


articles

Primary sequence information from intact proteins by electrospray ionization tandem mass spectrometry

JA Loo, CG Edmonds, and RD Smith

Chemical Sciences Department, Pacific Northwest Laboratory, Richland, WA 99352.

Tandem mass spectrometry has been used to obtain information related to portions of the primary sequence for an intact protein, bovine ribonuclease A. Multiply charged molecular ions, generated by electrospray ionization, were collisionally dissociated at low energies in a triple quadrupole mass spectrometer to yield singly and multiply charged fragment ions that can be assigned to the known sequence of the protein. Dissociation of the highly charged molecular ions resulted in pairs of complementary product ions. The higher order (gas-phase) protein structure affects the dissociation processes, as observed in comparisons of tandem mass spectra of the native and disulfide-reduced forms of ribonuclease A.


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