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Related Concept Videos

Intrinsically Disordered Proteins02:18

Intrinsically Disordered Proteins

Intrinsically disordered proteins are a group of proteins that do not fold into specific three-dimensional structures. Their structural flexibility allows them to complement ordered proteins to perform functions that are inaccessible to rigid structures. They are more common in eukaryotes than prokaryotes and may either be exclusively intrinsically disordered or hybrid proteins, consisting of a mix of ordered and disordered regions. The absence of a rigid structure in these proteins can be...
Peptide Identification Using Tandem Mass Spectrometry01:33

Peptide Identification Using Tandem Mass Spectrometry

Tandem mass spectrometry, also known as MS/MS or MS2, is an analytical technique that employs two mass analyzers. Essentially it is a series of mass spectrometers that helps isolate a particular biomolecule and then helps study its chemical properties.
This technique helps gather information regarding the protein from which the peptide was obtained and to study the peptides’ amino acid sequence. Identifying peptides from a complex mixture is an important component of the growing field of...
MALDI-TOF Mass Spectrometry01:19

MALDI-TOF Mass Spectrometry

Mass spectrometry is a powerful characterization technique that can identify and separate a wide variety of compounds ranging from chemical to biological entities, based on their mass-to-charge ratio (m/z). The instruments that allow this detection, known as mass spectrometers, have three components: an ion source, a mass analyzer, and a detector. These spectrometers differ based on the nature of their ion source and analyzers.Matrix-assisted laser desorption ionization (MALDI) is a commonly...
Mass Spectrometry: Complex Analysis01:21

Mass Spectrometry: Complex Analysis

Mass spectrometry is an important technique for the identification of pure compounds. However, it has some limitations for the analysis of complex mixtures, often due to excessive fragmentation making the spectrum too complicated to decipher. Mass spectrometry can be combined with suitable separation methods in sequence, forming hyphenated methods, which are useful in the analysis of complex mixtures.
GC–MS is a powerful hyphenated method commonly used in forensics and environmental...

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Related Experiment Video

Updated: May 17, 2026

Matrix-assisted Laser Desorption/Ionization Time of Flight (MALDI-TOF) Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa
07:49

Matrix-assisted Laser Desorption/Ionization Time of Flight (MALDI-TOF) Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa

Published on: September 9, 2013

Mass spectrometry methods for intrinsically disordered proteins.

Rebecca Beveridge1, Quentin Chappuis, Cait Macphee

  • 1School of Chemistry, University of Edinburgh, West Mains Road, Edinburgh EH9 3JJ, Scotland.

The Analyst
|October 31, 2012
PubMed
Summary
This summary is machine-generated.

Mass spectrometry, including ion mobility-mass spectrometry (IM-MS), offers powerful insights into intrinsically disordered proteins (IDPs) and their aggregation into amyloid fibrils linked to neurodegenerative diseases.

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

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Matrix-assisted Laser Desorption/Ionization Time of Flight (MALDI-TOF) Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa
07:49

Matrix-assisted Laser Desorption/Ionization Time of Flight (MALDI-TOF) Mass Spectrometric Analysis of Intact Proteins Larger than 100 kDa

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Combining Chemical Cross-linking and Mass Spectrometry of Intact Protein Complexes to Study the Architecture of Multi-subunit Protein Assemblies
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Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins
07:24

Paramagnetic Relaxation Enhancement for Detecting and Characterizing Self-Associations of Intrinsically Disordered Proteins

Published on: September 23, 2021

Area of Science:

  • Biophysics
  • Structural Biology
  • Proteomics

Background:

  • Intrinsically disordered proteins (IDPs) represent a significant subset of proteins with unique structural and dynamic properties.
  • Mass spectrometry (MS) has become a crucial biophysical technique for studying protein structure and dynamics.
  • IDPs present challenges to traditional structural biology methods due to their lack of stable tertiary structure.

Purpose of the Study:

  • To review the application of mass spectrometry (MS) and ion mobility-mass spectrometry (IM-MS) in the study of intrinsically disordered proteins (IDPs).
  • To highlight how MS-based techniques can validate biophysical hypotheses regarding IDP behavior.
  • To demonstrate the utility of IM-MS in characterizing IDP conformations and their aggregation pathways.

Main Methods:

  • Nano-electrospray ionization mass spectrometry (n-ESI-MS) to infer conformational ensembles in solution from charge state distributions.
  • Ion mobility-mass spectrometry (IM-MS) to measure collision cross-sections and correlate them with protein conformation.
  • Utilizing IM-MS to monitor the early stages of amyloid fibril formation by IDPs.

Main Results:

  • n-ESI-MS provides insights into the degree of protein folding in solution.
  • IM-MS allows for the determination of rotationally averaged collision cross-sections, aiding conformational analysis of IDPs.
  • IM-MS effectively characterizes monomer structure, oligomer distributions, and aggregation mechanisms relevant to neurodegenerative diseases.

Conclusions:

  • MS and IM-MS are powerful tools for investigating the structure, dynamics, and aggregation of intrinsically disordered proteins.
  • These techniques provide a means to experimentally test biophysical models of IDP behavior.
  • IM-MS offers valuable mechanistic insights into the early stages of amyloid formation, relevant to diseases like Parkinson's and Alzheimer's.