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Related Concept Videos

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...
Tandem Mass Spectrometry01:21

Tandem Mass Spectrometry

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...
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...
High-Resolution Mass Spectrometry (HRMS)01:15

High-Resolution Mass Spectrometry (HRMS)

The resolution of a mass spectrometer depends on the efficiency of separating ions with different ion masses. The mass of an atom is approximated to the sum of the masses of protons and neutrons inside, considering the masses of protons and neutrons as equal. However, the masses of the proton (1.6726 × 10−24 g) and neutron (1.6749 × 10−24 g) are not truly equal. There is a minor error in the expression of atomic masses relative to the simplest atom of hydrogen. For example, the mass of helium...
Mass Spectrometry: Molecular Fragmentation Overview01:20

Mass Spectrometry: Molecular Fragmentation Overview

The ionization of a molecule into a molecular ion inside the mass spectrometer causes instability in the molecule's structure due to the loss of an electron. This eventually leads to the fragmentation or breaking of some bonds in the molecule. The fragmentation occurs predominantly at specific bonds to yield relatively stable fragments.
One type of fragmentation pattern is the cleavage of a single bond in the molecular ion. The cleavage leads to a radical and a cation. The cleavage can occur at...
Mass Spectrum: Interpretation01:24

Mass Spectrum: Interpretation

An unknown compound can be established by identifying the molecular ion peak in the mass spectrum. The molecular ion peak is often weak or absent due to the predominance of fragmentation in high-energy electron beams. In such cases, a soft-energy electron beam can be used to scan the spectrum to enhance the intensity of the molecular ion peak. Additionally, chemical ionization, field ionization, and desorption ionization spectra are used to obtain a relatively intense molecular ion peak.To...

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Analyzing Large Protein Complexes by Structural Mass Spectrometry
15:35

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Published on: June 19, 2010

Dissecting heterogeneous molecular chaperone complexes using a mass spectrum deconvolution approach.

Florian Stengel1, Andrew J Baldwin, Matthew F Bush

  • 1Physical and Theoretical Chemistry Laboratory, Department of Chemistry, University of Oxford, Oxford OX1 3QZ, UK.

Chemistry & Biology
|May 29, 2012
PubMed
Summary

Small heat-shock proteins (sHSPs) prevent protein aggregation by binding targets. A new mass spectrometry algorithm reveals how sHSP complexes form, showing binding depends on target mass and preserves native structure.

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Analyzing Large Protein Complexes by Structural Mass Spectrometry
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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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Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry
10:24

Defining Hsp33's Redox-regulated Chaperone Activity and Mapping Conformational Changes on Hsp33 Using Hydrogen-deuterium Exchange Mass Spectrometry

Published on: June 7, 2018

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Structural Biology

Background:

  • Small heat-shock proteins (sHSPs) are crucial molecular chaperones.
  • sHSPs prevent protein aggregation by binding to nonnative target proteins.
  • The heterogeneous nature of sHSP:target complexes has hindered understanding of their organization.

Purpose of the Study:

  • To develop a novel algorithm for analyzing mass spectrometry data of heterogeneous protein assemblies.
  • To elucidate the stoichiometry and organization of complexes formed between sHSPs and various target proteins.
  • To understand the mechanism by which sHSPs protect proteins from denaturation.

Main Methods:

  • Development of a nanoelectrospray mass spectrometry analysis algorithm.
  • Estimation of stoichiometry distribution in polydisperse oligomer ensembles.
  • Analysis of sHSP complexes with different target proteins.

Main Results:

  • Binding of sHSPs to target proteins is mass-dependent.
  • Resultant sHSP:target complexes reflect the native quaternary architecture of the target protein.
  • Protein protection by sHSPs occurs early in the denaturation process.

Conclusions:

  • The developed algorithm accurately interprets mass spectra from heterogeneous protein assemblies.
  • The findings explain how sHSPs achieve protection through variable complex morphologies.
  • This approach is broadly applicable to studying other polydisperse protein systems.