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Related Concept Videos

Deconvolution01:20

Deconvolution

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Deconvolution, also known as inverse filtering, is the process of extracting the impulse response from known input and output signals. This technique is vital in scenarios where the system's characteristics are unknown, and they must be inferred from the observable signals.
Deconvolution involves several mathematical techniques to derive the impulse response. One common approach is polynomial division. In this method, the input and output sequences are treated as coefficients of...
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Mass Spectrometry: Overview01:19

Mass Spectrometry: Overview

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Mass spectrometry is an analytical technique used to determine the molecular mass and molecular formula of a compound. The basic principle of mass spectrometry is to generate ions from the analyte molecule and measure these ion abundances against their molecular mass. One common type of ionization, known as electron ionization or EI, bombards the analyte molecules in the gas phase with high-energy electron beams. The electron beams displace an electron from the molecule and leave behind a...
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Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

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Tandem mass spectrometry is a technique that uses multiple mass analyzers in series to obtain a higher selectivity and reduce chemical noise during analyte detection. Instruments with multiple analyzers separated by an interaction cell enable secondary fragmentation and selected study of the fragment ions.Secondary fragmentations occur in the interaction cell and can be induced by various factors. Fragmentation induced by collision with inert gases, such as N2, Ar, He, etc., is called...
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Mass Spectrometry of Amines01:15

Mass Spectrometry of Amines

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In mass spectroscopy, amines undergo fragmentation to give parent ions with odd molecule weights. This observed mass spectrum follows the nitrogen rule; a molecule with an odd number of nitrogen atoms produces a molecular ion with an odd molecular weight. Amines undergo fragmentation through α cleavage, producing nitrogen-containing cations—iminium ions—and alkyl radicals. Mass spectra of aromatic and cyclic aliphatic amines exhibit strong molecular ion peaks, but acyclic...
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Mass Spectrometry: Isotope Effect01:13

Mass Spectrometry: Isotope Effect

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Most elements exist in nature as a mixture of isotopes. The isotopes differ in weight due to their respective number of neutrons. The molecular weight of a molecule is different depending on the specific isotope of its elements involved. As a result, the mass spectrum of the molecule exhibits peaks from the same fragment at multiple positions. The positions of these mass signals depend on the mass differences between isotopes. Furthermore, the intensity of these signals is dependent on the...
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Ions and Ionic Charges03:27

Ions and Ionic Charges

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In ordinary chemical reactions, the nucleus — which contains the protons and neutrons of each atom and thus identifies the element — remains unchanged. Electrons, however, can be added to atoms by transfer from other atoms, lost by transfer to other atoms, or shared with other atoms. The transfer and sharing of electrons among atoms govern the chemistry of the elements. During the formation of some compounds, atoms gain or lose electrons to form electrically charged particles called...
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Related Experiment Video

Updated: Feb 15, 2026

Semi-Quantitative Analysis of Peptidoglycan by Liquid Chromatography Mass Spectrometry and Bioinformatics
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Parsimonious Charge Deconvolution for Native Mass Spectrometry.

Marshall Bern1, Tomislav Caval2, Yong J Kil1

  • 1Protein Metrics, Inc. , San Carlos, California 94070, United States.

Journal of Proteome Research
|January 30, 2018
PubMed
Summary
This summary is machine-generated.

A new parsimonious charge deconvolution algorithm reduces artifacts in mass spectrometry. This method enhances the analysis of intact glycoproteins and protein complexes using native mass spectrometry.

Keywords:
algorithmcetuximabdaclizumabfactor Pglycoproteinhigh-resolution native mass spectrometryinfliximabintact massmaximum entropymonoclonal antibodyparsimonyproperdin

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Resolving Affinity Purified Protein Complexes by Blue Native PAGE and Protein Correlation Profiling
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Area of Science:

  • Biochemistry
  • Analytical Chemistry
  • Proteomics

Background:

  • Charge deconvolution algorithms infer molecular mass from mass-over-charge (m/z) data in electrospray ionization mass spectra.
  • Common algorithms like MaxEnt can introduce artifacts, such as incorrect mass assignments (e.g., half or one-third of the true mass), particularly over wide m/z ranges or broad target mass ranges.
  • Existing methods struggle with native mass spectrometry data due to challenges like salt adducts, multimers, and lower charge states.

Purpose of the Study:

  • To introduce a novel "parsimonious" charge deconvolution algorithm designed to minimize artifacts.
  • To demonstrate the algorithm's suitability for high-resolution native mass spectrometry of intact proteins and protein complexes.
  • To improve the accuracy and interpretability of mass spectrometry data for complex biological molecules.

Main Methods:

  • Development of a new parsimonious charge deconvolution algorithm with a modified objective function to favor simpler spectral interpretations.
  • Application and validation of the algorithm on diverse biological samples, including heavily glycosylated proteins and therapeutic antibodies.
  • Comparison of results with existing methods and manual analysis of m/z peaks.

Main Results:

  • The parsimonious algorithm successfully produced fewer artifacts compared to traditional methods.
  • Simultaneous deconvolution of monomer and dimer species was achieved for the plasma properdin glycoprotein.
  • Accurate glycoform masses were determined for properdin, enabling analysis previously requiring manual interpretation.
  • Facilitated analysis of modifications like extensions, truncations, and glycosylation on therapeutic antibodies.

Conclusions:

  • The parsimonious charge deconvolution algorithm offers improved accuracy and reduced artifacts for native mass spectrometry.
  • This new algorithm is particularly effective for analyzing intact glycoproteins and protein complexes.
  • It enhances the utility of native mass spectrometry for both qualitative and quantitative analyses of proteins and protein assemblies.