Trapping, Detection, and Mass Determination of Coliphage T4 DNA Ions by Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Chen, Ruidan.; Cheng, Xueheng; Mitchell, Dale W.; Hofstadler, Steven A.; Wu, Qi; Rockwood, Alan L.; Sherman, Michael G.; Smith, Richard D.

doi:10.1021/ac00103a004

Cited by 153 publications

(143 citation statements)

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“…The growing interest in mass spectrometry of noncovalent protein complexes and nucleic acids in the early 1990s prompted the Smith group to develop a Fourier transform ion cyclotron resonance (FTICR) approach that was able to trap single, MDa-size DNA ions and simultaneously measure their m/z and z [8]. In this approach, charges states as low as +30 were detected with a precision of ±10%.…”

Section: Harge Detection Mass Spectrometry (Cdms) Is a Techniquementioning

confidence: 99%

Charge Detection Mass Spectrometry for Single Ions with an Uncertainty in the Charge Measurement of 0.65 e

Pierson

Contino

Keifer

et al. 2015

J. Am. Soc. Mass Spectrom.

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Abstract. Charge detection mass spectrometry (CDMS) provides a direct measure of the mass of individual ions through nondestructive, simultaneous measurements of the mass to charge ratio and the charge. To improve the accuracy of the charge measurement, ions are trapped and recirculated through the charge detector. By substantially extending the trapping time, the uncertainty in the charge determination has been reduced by a factor of two, from 1.3 elementary charges (e) to 0.65 e. The limit of detection (the smallest charge that can be reliably measured) has been reduced by about the same proportion, from 13 to 7 e. The more precise charge measurements enable a substantial improvement in the mass resolution, which is critical for applications of CDMS to mixtures of high mass ions.

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Section: Harge Detection Mass Spectrometry (Cdms) Is a Techniquementioning

confidence: 99%

Charge Detection Mass Spectrometry for Single Ions with an Uncertainty in the Charge Measurement of 0.65 e

Pierson

Contino

Keifer

et al. 2015

J. Am. Soc. Mass Spectrom.

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“…In comparison to MALDI MS, molecular weight measurements with higher resolution and mass accuracy of PCR products has been achieved using ESI in conjunction with Fourier transform ion cyclotron resonance (FTICR) MS (29)(30)(31)(32)(33)(34). Furthermore, new technical developments for molecular weight measurement allow the detection of DNA molecules as large as 110 MDa by ESI MS (35)(36)(37).…”

Section: Introductionmentioning

confidence: 99%

Analysis of short tandem repeat polymorphisms by electrospray ion trap mass spectrometry

Hahner¹

2000

Nucleic Acids Research

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The application of electrospray ionization (ESI) ion trap mass spectrometry (MS) to the analysis of short tandem repeats (STRs or microsatellites) is described. Several equine dinucleotide STR loci were chosen as a model system to evaluate ESI ion trap as a routine instrument for rapid and reliable genoytping. With the use of specific primers STR loci were amplified from different blood samples having allele sizes between 60 and 100 bp. A new purification method based on reversible binding of PCR products to magnetic particles has proven to be directly compatible with ESI ion trap MS analysis. The sense and antisense strands of the PCR products with concentrations of ∼100 fmol/µl were measured with a mass accuracy of 0.01%. The simplicity of the purification method and the capability for automated handling together with the precise sizing of PCR products by ESI ion trap MS facilitate the large scale analysis of polymorphic STRs. Moreover, mixtures of different allele length as obtained for heterozygous samples could accurately be assigned as well as a C→G switch between the two strands of a PCR product.

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“…These applications have driven mass spectrometry to new levels of detection from a range of complex biological matrices. In addition, highresolution ion cyclotron resonance mass spectrometry has enabled the isolation of individual ions from polyethylene glycol (7) and DNA (8), with masses in excess of 10 8 Da. As well as being able to characterize highly charged polymers, it has been possible to detect signals from noncovalent complexes of small molecule ligands bound to proteins and of multiprotein complexes (9,10).…”

mentioning

confidence: 99%

Detection and selective dissociation of intact ribosomes in a mass spectrometer

Rostom

Fucini²,

Benjamin³

et al. 2000

Proc. Natl. Acad. Sci. U.S.A.

201

174

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Intact Escherichia coli ribosomes have been projected into the gas phase of a mass spectrometer by means of nanoflow electrospray techniques. Species with mass͞charge ratios in excess of 20,000 were detected at the level of individual ions by using time-of-flight analysis. Once in the gas phase the stability of intact ribosomes was investigated and found to increase as a result of cross-linking ribosomal proteins to the rRNA. By lowering the Mg 2؉ concentration in solutions containing ribosomes the particles were found to dissociate into 30S and 50S subunits. The resolution of the charge states in the spectrum of the 30S subunit enabled its mass to be determined as 852,187 ؎ 3,918 Da, a value within 0.6% of that calculated from the individual proteins and the 16S RNA. Further dissociation into smaller macromolecular complexes and then individual proteins could be induced by subjecting the particles to increasingly energetic gas phase collisions. The ease with which proteins dissociated from the intact species was found to be related to their known interactions in the ribosome particle. The results show that emerging mass spectrometric techniques can be used to characterize a fully functional biological assembly as well as its isolated components. In recent years mass spectrometry has become the method of choice for a number of important aspects of experimental structural biology. These include: the characterization of the stability and folding behavior of proteins under a wide range of conditions (1-3), the identification of subpicomole quantities of proteins from two-dimensional gels (4), the de novo sequencing of peptides and subsequent cloning of novel proteins (5), and the analysis of the components of single vesicles (6). These applications have driven mass spectrometry to new levels of detection from a range of complex biological matrices. In addition, highresolution ion cyclotron resonance mass spectrometry has enabled the isolation of individual ions from polyethylene glycol (7) and DNA (8), with masses in excess of 10 8 Da. As well as being able to characterize highly charged polymers, it has been possible to detect signals from noncovalent complexes of small molecule ligands bound to proteins and of multiprotein complexes (9, 10). As the size of such assemblies increases, however, the number of charges acquired during the electrospray process increases less rapidly than the total mass. This phenomenon has been attributed to ionic interactions in the intermolecular interfaces and the appropriation of negatively charged counterions from the volatile buffers used in the analysis of such species (11). The net result of these effects is that large multimolecular complexes, such as the 2.3-MDa ribosome, have been outside the mass range of conventional mass spectrometers. In previous mass spectrometry experiments disruption of the ribosome enabled the identification of the contact sites between ribosomal proteins and RNA (12) and a novel protein component from the Saccharomyces cerevsiae ribosome (13). In add...

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Trapping, Detection, and Mass Determination of Coliphage T4 DNA Ions by Electrospray Ionization Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Cited by 153 publications

References 0 publications

Charge Detection Mass Spectrometry for Single Ions with an Uncertainty in the Charge Measurement of 0.65 e

Charge Detection Mass Spectrometry for Single Ions with an Uncertainty in the Charge Measurement of 0.65 e

Analysis of short tandem repeat polymorphisms by electrospray ion trap mass spectrometry

Detection and selective dissociation of intact ribosomes in a mass spectrometer

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