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Related Concept Videos

X-ray Diffraction of Biological Samples01:10

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X-ray diffraction or XRD is an analytical tool that utilizes X-rays to study ordered structures such as crystalline organic and inorganic samples, polycrystalline materials, proteins, carbohydrates, and drugs.
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¹H NMR Signal Multiplicity: Splitting Patterns01:13

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When protons A and X are coupled, their nuclear spin energy levels are slightly modified. This is because the energy required to excite proton A to a spin state parallel to proton X is slightly different from the energy required for it to become anti-parallel to spin X. Consequently, there are two possible excitation frequencies for A (A1 and A2), depending on the spin state of X, and vice versa. The mutual nature of coupling implies that the difference between frequencies A1 and A2, indicated...
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¹H NMR: Complex Splitting01:13

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A proton M that is coupled to a proton X results in doublet signals for M. However, NMR-active nuclei can be simultaneously coupled to more than one nonequivalent nucleus. When M is coupled to a second proton A, such as in styrene oxide, each peak in the doublet is split into another doublet.
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The size of the unit cell and the arrangement of atoms in a crystal may be determined from measurements of the diffraction of X-rays by the crystal, termed X-ray crystallography.
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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.
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To Cleave or Not To Cleave in XL-MS?

B Steigenberger1,2, P Albanese1,2, A J R Heck1,2

  • 1Biomolecular Mass Spectrometry and Proteomics, Bijvoet Center for Biomolecular Research and Utrecht Institute for Pharmaceutical Sciences , Utrecht University , Padualaan 8 , 3584 CH Utrecht , The Netherlands.

Journal of the American Society for Mass Spectrometry
|February 8, 2020
PubMed
Summary
This summary is machine-generated.

Cross-linking mass spectrometry (XL-MS) reveals protein structures and interactions. This review analyzes a decade of XL-MS literature to identify dominant workflows for researchers.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Proteomics

Background:

  • Cross-linking mass spectrometry (XL-MS) provides distance constraints for in-solution protein structures.
  • XL-MS complements techniques like X-ray crystallography and cryo-EM.
  • A wide variety of cross-linking reagents exist, complicating experimental design.

Purpose of the Study:

  • To review and identify predominant cross-linking mass spectrometry (XL-MS) workflows from the past decade.
  • To guide researchers in selecting appropriate XL-MS methods for their experiments.
  • To highlight widely used approaches in application-focused XL-MS literature.

Main Methods:

  • Systematic review of published XL-MS application papers from the last 10 years.
  • Extraction of data on sample types, cross-linking reagents, prefractionation, instrumentation, and data analysis.
  • Synthesis of findings into a decision-making flowchart for experimental design.

Main Results:

  • Identification of predominantly applied workflows in XL-MS based on literature analysis.
  • Summary of common practices in sample preparation, reagent choice, and data processing.
  • Development of a flowchart to aid novice researchers in selecting XL-MS strategies.

Conclusions:

  • The analysis provides an overview of established XL-MS workflows.
  • The developed flowchart serves as a practical guide for researchers entering the field.
  • This resource aims to facilitate the application of XL-MS for studying protein structure and interactions.