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¹H NMR of Labile Protons: Temporal Resolution01:10

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Protons bonded to heteroatoms such as nitrogen and oxygen exhibit a range of chemical shift values. This is due to the varying degree of hydrogen bonding between the proton and the heteroatom in other molecules. The extent of hydrogen bonding affects the electron density around the proton, thereby giving different chemical shift values for the protons in the proton NMR spectrum.
The –OH proton in alcohols typically appears in the range of δ 2 to 5 ppm but can vary depending on the specific...
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Related Experiment Video

Updated: Apr 2, 2026

Temporal Ordering of Dynamic Expression Data from Detailed Spatial Expression Maps
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Culturing a discerning palette for spatiofunctional profiling.

Marcus J C Long1, Xin Liang2, Yimon Aye3

  • 1Department of Pharmacology, University of Oxford, Oxford, OX1 3QT, United Kingdom; Department of Chemistry, University of Oxford, Oxford, OX1 3TA, United Kingdom.

Current Opinion in Chemical Biology
|March 31, 2026
PubMed
Summary
This summary is machine-generated.

Spatiofunctional profiling uses novel metabolites to identify and target proteins in specific cellular locations. This method enables functional studies by revealing proteins amenable to chemical manipulation within distinct cellular compartments.

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Area of Science:

  • Proteomics and Chemical Biology
  • Cellular Biology and Biochemistry

Background:

  • Proteomics innovations allow protein localization studies, but lack mechanistic insights.
  • Current spatial data does not guide functional perturbation of proteins in specific cellular regions.

Purpose of the Study:

  • Introduce spatiofunctional profiling to link protein localization with functional manipulation.
  • Develop a strategy to identify proteins susceptible to chemical modification within specific cellular locales.

Main Methods:

  • Utilize (preter)natural metabolites as probes for spatiofunctional profiling.
  • Census proteins engaging with small-molecule ligands in defined cellular compartments.

Main Results:

  • Demonstrated the ability to index proteins within specific locales based on ligand engagement.
  • Showcased the potential for chemical manipulation of localized proteins.

Conclusions:

  • Spatiofunctional profiling offers a novel approach to study protein function in situ.
  • This strategy bridges spatial proteomics and targeted chemical biology for mechanistic investigations.