NDLI: Counting individual sulfur atoms in a protein byultrahighresolution Fourier transform ion cyclotron resonance mass spectrometry: Experimental resolution of isotopic finestructure in proteins

Content Provider	PubMed Central
Author	Shi, Stone D. H. Hendrickson, Christopher L. Marshall, Alan G.
Copyright Year	1998
Abstract	A typical molecular ion mass spectrum consists of a sum of signalsfrom species of various possible isotopic compositions. Only themonoisotopic peak (e.g., all carbons are 12C; all nitrogensare 14N, etc.) has a unique elemental composition. Everyother isotope peak at approximately integer multiples of ∼1 Da higherin nominal mass represents a sum of contributions from isotopecombinations differing by a few mDa (e.g., two 13C vs. two15N vs. one 13C and one 15N vs.34S, vs. 18O, etc., at ∼2 Da higher in massthan the monoisotopic mass). At sufficiently high mass resolving power,each of these nominal-mass peaks resolves into its isotopic finestructure. Here, we report resolution of the isotopic fine structure ofproteins up to 15.8 kDa (isotopic 13C,15Ndoubly depleted tumor suppressor protein, p16), made possible byelectrospray ionization followed by ultrahigh-resolution Fouriertransform ion cyclotron resonance mass analysis at 9.4 tesla. Further,a resolving power of m/Δm50% ≈8,000,000 has beenachieved on bovine ubiquitin (8.6 kDa). These results represent a10-fold increase in the highest mass at which isotopic fine structurepreviously had been observed. Finally, because isotopic fine structurereveals elemental composition directly, it can be used to confirm ordetermine molecular formula. For p16, for example, we were able todetermine (5.1 ± 0.3) the correct number (five) of sulfur atomssolely from the abundance ratio of the resolved 34S peak tothe monoisotopic peak.
Starting Page	11532
File Format	PDF
ISSN	10916490
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	20
Volume Number	95
Language	English
Publisher	National Academy of Sciences
Publisher Date	1998-09-29
Access Restriction	Open
Rights Holder	National Academy of Sciences
Subject Keyword	Research in Higher Education
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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