The Production of High Speed Light Ions Without the Use of High Voltages

Lawrence, Ernest Orlando; Livingston, M. Stanley

doi:10.1103/physrev.40.19

Cited by 248 publications

(71 citation statements)

References 14 publications

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“…The cyclotron principle, the core of Fourier transform ion cyclotron resonance mass spectrometry, was introduced by E. O. Lawrence in the early 1931 [30] and in 1936, F. M. Penning added an electrostatic confinement perpendicular to the magnetic field [31], a construction that later became known as the "Penning trap". As part of the Manhattan project during World War II, Lawrence converted a cyclotron into a mass spectrograph (or a 180° magnetic sector) and used this in a preparative mode to separate 235 U from 238 U.…”

Section: Figurementioning

confidence: 99%

Identification and Characterization of Peptides and Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Palmblad

Bergquist

2003

Journal of Chromatography Library

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Mass spectrometry has in recent years been established as the standard method for protein identification and characterization in proteomics with excellent intrinsic sensitivity and specificity. Fourier transform ion cyclotron resonance is the mass spectrometric technique that provides the highest resolving power and mass accuracy, increasing the amount of information that can be obtained from complex samples. This thesis concerns how useful information on proteins of interest can be extracted from mass spectrometric data on different levels of protein structure and how to obtain this data experimentally. It was shown that it is possible to analyze complex mixtures of protein tryptic digests by direct infusion electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry and identify abundant proteins by peptide mass fingerprinting. Coupling on-line methods such as liquid chromatography and capillary electrophoresis increased the number of proteins that could be identified in human body fluids. Protein identification was also improved by novel statistical methods utilizing prediction of chromatographic behavior and the non-randomness of enzymatic digestion. To identify proteins by short sequence tags, electron capture dissociation was implemented, improved and finally coupled on-line to liquid chromatography for the first time. The combined techniques can be used to sequence large proteins de novo or to localize and characterize any labile post-translational modification. New computer algorithms for the automated analysis of isotope exchange mass spectra were developed to facilitate the study of protein structural dynamics. The non-covalent interaction between HIV-inhibitory peptides and the oligomerization of amyloid β-peptides were investigated, reporting several new findings with possible relevance for development of anti-HIV drug therapies and understanding of fundamental mechanisms in Alzheimer's disease.

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Section: Figurementioning

confidence: 99%

Identification and Characterization of Peptides and Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Palmblad

Bergquist

2003

Journal of Chromatography Library

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“…As early as 1926, H. Blumgart developed a radiotracer technique to measure blood flow velocity which is the forerunner of dynamic tracer studies [44] . De Hevesy introduced the red cell blood volume measurement and the 'dilution principle' in humans using the first man-made radioisotope 32 P produced by the cyclotron in Berkeley, a milestone invention by E. O. Lawrence in 1931 for which he received the Nobel Prize in 1939 [43,45] . With the cyclotron it was now possible to artificially produce radiopharmaceuticals and radionuclides, which became increasingly available for clinical research.…”

Section: Nuclear Imagingmentioning

confidence: 99%

Seeing the heart; the success story of cardiac imaging

Roelandt¹

2000

European Heart Journal

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“…A forerunner in this pursuit was Ernest Lawrence, who -inspired by an article reporting on a three-stage accelerator for sodium ions [3] -wondered if instead of building many acceleration stages in a line, one should re-use an acceleration field by circulating positive ions back through it with the help of a magnetic field. With this novel thought, the cyclotron was born [4]. The energy that could be achieved with a cyclotron was about 15 MeV.…”

Section: Introductionmentioning

confidence: 99%

A synchrotron for neutral molecules

Heiner

Bethlem

Meijer

2009

Chemical Physics Letters

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Here we report on a synchrotron for neutral molecules that consists of two hexapole focusers bent into a torus. By switching the voltages applied to the two half-rings, polar molecules can be confined in tight packets for up to a second as they revolve around the ring. In this article, the operation and trapping parameters of the molecular synchrotron are discussed. We plan to use a molecular synchrotron in the future as an arena for low-energy collision experiments.

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The Production of High Speed Light Ions Without the Use of High Voltages

Cited by 248 publications

References 14 publications

Identification and Characterization of Peptides and Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Identification and Characterization of Peptides and Proteins Using Fourier Transform Ion Cyclotron Resonance Mass Spectrometry

Seeing the heart; the success story of cardiac imaging

A synchrotron for neutral molecules

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