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Characterization of Protein Glycoforms at Intact Level by Orbitrap Mass Spectrometry

2021
Intact mass analysis of proteins is simple, fast, and specific, and it effectively provides structural insight into the proteoforms or variants of the analyzed protein. For instance, the multiple glycoforms of recombinant monoclonal antibodies can be effectively analyzed by intact mass spectrometry (MS).
Dan Bach, Kristensen   +3 more
openaire   +2 more sources

Native protein mass spectrometry: from intact oligomers to functional machineries

Current Opinion in Chemical Biology, 2004
The development of electrospray ionization coupled to mass spectrometry has enabled the analysis of very large intact protein complexes, even when they are held together by weak non-covalent interactions. Together with equally spectacular advances in mass spectrometric instrumentation, a new field has emerged, termed native protein mass spectrometry ...
van den Heuvel, R.H.H., Heck, A.J.R.
openaire   +3 more sources

Intact mass spectrometry screening to optimize hydroxyl radical dose for protein footprinting

Biochemical and Biophysical Research Communications, 2023
Hydroxyl radical protein footprinting (HRPF) using synchrotron radiation is a well-validated method to assess protein structure in the native solution state. In this method, X-ray radiolysis of water generates hydroxyl radicals that can react with solvent accessible side chains of proteins, with mass spectrometry used to detect the resulting labeled ...
Erik R. Farquhar   +5 more
openaire   +2 more sources

Liquid Extraction Surface Analysis Mass Spectrometry Imaging of Denatured Intact Proteins

2023
Liquid extraction surface analysis (LESA) is an ambient surface sampling technique that can be coupled with mass spectrometry (MS) to analyze analytes directly from biological substrates such as tissue sections. LESA MS involves liquid microjunction sampling of a substrate by use of a discrete volume of solvent followed by nano-electrospray ionization.
Emma K, Sisley   +3 more
openaire   +2 more sources

Capillary electrophoresis–mass spectrometry for the analysis of intact proteins 2007–2010

ELECTROPHORESIS, 2010
AbstractCE coupled to MS has proven to be a powerful analytical tool for the characterization of intact proteins, as it combines the high separation efficiency of CE with the selectivity of MS. This review provides an overview of the development and application of CE‐MS methods within the field of intact protein analysis as published between January ...
Haselberg, R.   +2 more
openaire   +4 more sources

Absolute venomics: Absolute quantification of intact venom proteins through elemental mass spectrometry

Journal of Proteomics, 2017
We report the application of a hybrid element and molecular MS configuration for the parallel absolute quantification of μHPLC-separated intact sulfur-containing venom proteins, via ICP triple quadrupole MS and 32S/34S isotope dilution analysis, and identification by ESI-QToF-MS of the toxins of the medically important African black-necked spitting ...
Francisco Calderón-Celis   +4 more
openaire   +2 more sources

Evaluation of Intact Mass Spectrometry for the Quantitative Analysis of Protein Therapeutics

Analytical Chemistry, 2012
Implementation of modern analytical techniques, such as intact mass spectrometry, may allow for more detailed quality assessments of protein therapeutics. The complexity of the protein therapeutic manufacturing process as well as the sensitivity of these drugs to different storage conditions can lead to the presence of several undesired products ...
Ashley C, Gucinski, Michael T, Boyne
openaire   +2 more sources

Multiplexed Size Separation of Intact Proteins in Solution Phase for Mass Spectrometry

Analytical Chemistry, 2009
Reliable size-based protein separation is an invaluable biological technique. Unfortunately, size separation in solution is underutilized, owing perhaps to the poor resolution of conventional techniques. Here, we report an enhanced multiplexed GELFrEE (gel-eluted liquid fraction entrapment electrophoresis) device which incorporates eight independent ...
John C, Tran, Alan A, Doucette
openaire   +2 more sources

Primary Sequence Information from Intact Proteins by Electrospray Ionization Tandem Mass Spectrometry

Science, 1990
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 ...
J A, Loo, C G, Edmonds, R D, Smith
openaire   +2 more sources

Mass Spectrometry of Intact Proteins from Two-Dimensional PAGE

2000
Many important cellular processes depend on co- and post-translational modifications of proteins. These alterations, which can affect the size, charge, conformation and the stability of proteins, not only increase the number of different protein species per cell, but also add to the complexity of the cellular protein pattern, hence, making proteome ...
Ch. Eckerskorn, K. Strupat
openaire   +1 more source

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