From large analogical instruments to small digital black boxes: 40 years of progress in mass spectrometry and its role in proteomics. Part I 1965–1984

Gelpí, E.

doi:10.1002/jms.1403

Cited by 18 publications

(11 citation statements)

References 104 publications

(109 reference statements)

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“…In general terms, mass spectrometers measure the mass to charge ( m / z ) ratio of charged molecules in gas phase, allowing for the determination of their molecular masses after charge state resolution. Over the years, several improvements to mass spectrometers have made the analysis of large molecules, such as peptide or proteins, possible (see [] for a historical perspective). While mass spectrometric analysis of intact proteins is feasible [], in most cases, identification of proteins by MS first involves proteolysis with a site‐specific enzyme to generate peptides.…”

Section: Identification Of Proteins By Mass Spectrometry (Ms)mentioning

confidence: 99%

Affinity‐purification coupled to mass spectrometry: Basic principles and strategies

2012

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Identifying the interactions established by a protein of interest can be a critical step in understanding its function. This is especially true when an unknown protein of interest is demonstrated to physically interact with proteins of known function. While many techniques have been developed to characterize protein-protein interactions, one strategy that has gained considerable momentum over the past decade for identification and quantification of protein-protein interactions, is affinity-purification followed by mass spectrometry (AP-MS). Here, we briefly review the basic principles used in affinity-purification coupled to mass spectrometry, with an emphasis on tools (both biochemical and computational), which enable the discovery and reporting of high quality protein-protein interactions.

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Section: Identification Of Proteins By Mass Spectrometry (Ms)mentioning

confidence: 99%

Affinity‐purification coupled to mass spectrometry: Basic principles and strategies

2012

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“…Brunnee covers the principles of common mass analyzers in a vibrant 1987 review [1]. Gelpi discusses over 130 different mass spectrometers built since 1965 in a series of two reviews [2, 3]. Only one totally new mass spectrometer type, the Orbitrap analyzer [4, 5], has been developed lately.…”

Section: Mass Spectral Instrumentation and Ionization Techniquesmentioning

confidence: 99%

“…Other hybrid instrument types are discussed in Ref. [2, 3]. Orthogonal or hybrid mass spectrometers are favorable for structural elucidation because they either increase the total peak resolution or they introduce another separation dimension that can be used either to trigger or acquire additional mass spectrometric information [89, 90].…”

Section: Mass Spectral Instrumentation and Ionization Techniquesmentioning

confidence: 99%

Advances in structure elucidation of small molecules using mass spectrometry

2010

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The structural elucidation of small molecules using mass spectrometry plays an important role in modern life sciences and bioanalytical approaches. This review covers different soft and hard ionization techniques and figures of merit for modern mass spectrometers, such as mass resolving power, mass accuracy, isotopic abundance accuracy, accurate mass multiple-stage MS(n) capability, as well as hybrid mass spectrometric and orthogonal chromatographic approaches. The latter part discusses mass spectral data handling strategies, which includes background and noise subtraction, adduct formation and detection, charge state determination, accurate mass measurements, elemental composition determinations, and complex data-dependent setups with ion maps and ion trees. The importance of mass spectral library search algorithms for tandem mass spectra and multiple-stage MS(n) mass spectra as well as mass spectral tree libraries that combine multiple-stage mass spectra are outlined. The successive chapter discusses mass spectral fragmentation pathways, biotransformation reactions and drug metabolism studies, the mass spectral simulation and generation of in silico mass spectra, expert systems for mass spectral interpretation, and the use of computational chemistry to explain gas-phase phenomena. A single chapter discusses data handling for hyphenated approaches including mass spectral deconvolution for clean mass spectra, cheminformatics approaches and structure retention relationships, and retention index predictions for gas and liquid chromatography. The last section reviews the current state of electronic data sharing of mass spectra and discusses the importance of software development for the advancement of structure elucidation of small molecules.Electronic supplementary materialThe online version of this article (doi:10.1007/s12566-010-0015-9) contains supplementary material, which is available to authorized users.

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“…Sin embargo, no fue hasta la invención de las llamadas técnicas de ionización suave MALDI (por las siglas en inglés de Matrix-assisted laser desorption/ionization [desorción/ionización por láser asistida por matriz]) y ESI (por las siglas en inglés de Electrospray ionization [ionización por electrospray]) 5,6 que esta tecnología empezó a utilizarse en los laboratorios para aplicaciones rutinarias. Estas técnicas de ionización suave permitieron el análisis de proteínas de elevado peso molecular y a la vez facilitaron el análisis de mezclas, ya que mediante estas técnicas los componentes de una mezcla compleja se ionizan sin sufrir apenas fragmentaciones, lo cual simplifica los espectros de masas 7 . En los últimos 20 años, estas nuevas técnicas de EM se convirtieron en indispensables para el avance de la proteómica, sobre todo al ser combinadas con el analizador de masas tipo TOF (por sus siglas en inglés de Time-of-flight [tiempo de vuelo]).…”

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