Jove
Visualize
Contact Us
JoVE
x logofacebook logolinkedin logoyoutube logo
ABOUT JoVE
OverviewLeadershipBlogJoVE Help Center
AUTHORS
Publishing ProcessEditorial BoardScope & PoliciesPeer ReviewFAQSubmit
LIBRARIANS
TestimonialsSubscriptionsAccessResourcesLibrary Advisory BoardFAQ
RESEARCH
JoVE JournalMethods CollectionsJoVE Encyclopedia of ExperimentsArchive
EDUCATION
JoVE CoreJoVE BusinessJoVE Science EducationJoVE Lab ManualFaculty Resource CenterFaculty Site
Terms & Conditions of Use
Privacy Policy
Policies

Related Concept Videos

¹H NMR: Complex Splitting01:13

¹H NMR: Complex Splitting

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.
Splitting diagrams or splitting tree diagrams are routinely used to depict such complex couplings. While drawing splitting diagrams, the splitting with the larger coupling constant is usually applied first.
Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule01:10

Interpreting ¹H NMR Signal Splitting: The (n + 1) Rule

In the AX proton spin system, proton A can sense the two spin states of a coupled proton X, resulting in a doublet NMR signal with two peaks of equal (1:1) intensity. When proton A is coupled to two equivalent protons (AX2 spin system), the spin states of each X can be aligned with or against the external field, creating three possible scenarios. This results in a 1:2:1  triplet signal, where the central peak corresponds to the chemical shift of A and is twice as large or intense as the others.
Cooperative Allosteric Transitions01:58

Cooperative Allosteric Transitions

Cooperative allosteric transitions can occur in multimeric proteins, where each subunit of the protein has its own ligand-binding site. When a ligand binds to any of these subunits, it triggers a conformational change that affects the binding sites in the other subunits; this can change the affinity of the other sites for their respective ligands. The ability of the protein to change the shape of its binding site is attributed to the presence of a mix of flexible and stable segments in the...
¹H NMR Signal Multiplicity: Splitting Patterns01:13

¹H NMR Signal Multiplicity: Splitting Patterns

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...
Protein Complexes with Interchangeable Parts01:57

Protein Complexes with Interchangeable Parts

Groups of proteins may form a complex where each protein in this complex has a different role in the overall execution of the complex’s function. Often some of the proteins in the complex can be replaced by a closely related variant to give a complex that contains many of the same components yet is functionally distinct.
The SCF ubiquitin ligase is a protein complex of five individual proteins. This complex attaches ubiquitin to other target proteins to mark them for degradation. In order to...
Spin–Spin Coupling Constant: Overview01:08

Spin–Spin Coupling Constant: Overview

In bromoethane, the three methyl protons are coupled to the two methylene protons that are three bonds away. In accordance with the n+1 rule, the signal from the methyl protons is split into three peaks with 1:2:1 relative intensities. The methylene protons appear as a quartet, with the relative intensities of 1:3:3:1.
Qualitatively, any spin plus-half nucleus polarizes the spins of its electrons to the minus-half state. Consequently, the paired electron in the hydrogen–carbon bond must have a...

You might also read

Related Articles

Articles linked to this work by shared authors, journal, and citation graph.

Sort by
Same author

Stabilizing Ni-O Through Bi Doping in LaNiO<sub>3</sub> Perovskite Oxide for Efficient Anion Exchange Membrane Water Electrolysis.

ChemSusChem·2026
Same author

Publisher Correction: In situ nanocrystal confinement for efficient blue perovskite LEDs.

Nature·2026
Same author

Spatial double-shelled structure achieving stable anion exchange membrane water electrolysis via enhanced local alkalinity.

Science advances·2026
Same author

In situ nanocrystal confinement for efficient blue perovskite LEDs.

Nature·2026
Same author

Atomic-scale revelation of in situ reverse regulation from particles to clusters in the Ni/La-CeO<sub>x</sub> catalyst.

Nature communications·2026
Same author

Interface-enhanced Ni<sub>3</sub>S<sub>2</sub>/LaNiO<sub>3</sub> heterostructure for efficient water oxidation.

Chemical communications (Cambridge, England)·2026

Related Experiment Video

Updated: May 21, 2026

Genetic Barcoding with Fluorescent Proteins for Multiplexed Applications
13:14

Genetic Barcoding with Fluorescent Proteins for Multiplexed Applications

Published on: April 14, 2015

2:1 multiplexing function in a simple molecular system.

Sha Xu1, Yu-Xin Hao, Wei Sun

  • 1School of Chemical Biology and Pharmaceutical Sciences, Capital Medical University, Beijing 100069, China. xusha0810@126.com

Sensors (Basel, Switzerland)
|June 6, 2012
PubMed
Summary

This study demonstrates a molecular 2:1 multiplexer using a fluorescent molecule. The system selectively reports inputs by controlling photo-induced electron transfer (PET) through protonation or metal ion chelation.

Keywords:
anthracenefluorescencemolecular 2:1 multiplexer

More Related Videos

Multiplex Chemical Imaging Based on Broadband Stimulated Raman Scattering Microscopy
09:57

Multiplex Chemical Imaging Based on Broadband Stimulated Raman Scattering Microscopy

Published on: July 25, 2022

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry
06:39

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry

Published on: January 26, 2024

Related Experiment Videos

Last Updated: May 21, 2026

Genetic Barcoding with Fluorescent Proteins for Multiplexed Applications
13:14

Genetic Barcoding with Fluorescent Proteins for Multiplexed Applications

Published on: April 14, 2015

Multiplex Chemical Imaging Based on Broadband Stimulated Raman Scattering Microscopy
09:57

Multiplex Chemical Imaging Based on Broadband Stimulated Raman Scattering Microscopy

Published on: July 25, 2022

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry
06:39

Analysis of Protein Complex Formation at Micromolar Concentrations by Coupling Microfluidics with Mass Photometry

Published on: January 26, 2024

Area of Science:

  • Supramolecular Chemistry
  • Fluorescence Spectroscopy
  • Molecular Recognition

Background:

  • Photo-induced electron transfer (PET) often quenches fluorescence in molecular systems.
  • Controlling PET is key to developing responsive molecular sensors and logic gates.
  • Anthracene derivatives are widely studied for their photophysical properties.

Purpose of the Study:

  • To design and demonstrate a molecular 2:1 multiplexer based on fluorescence.
  • To investigate the modulation of photo-induced electron transfer (PET) in a thiosemicarbazide-anthracene system.
  • To achieve selective input reporting through chemical stimuli.

Main Methods:

  • Synthesis of 1-[(Anthracen-9-yl)methylene] thiosemicarbazide.
  • Fluorescence spectroscopy to monitor emission changes.
  • Protonation and metal ion chelation as external stimuli.

Main Results:

  • The compound exhibits weak fluorescence due to PET from thiosemicarbazide to anthracene.
  • Protonation of the amine group restores fluorescence by suppressing PET.
  • Chelation with metal ions also suppresses PET, leading to fluorescence enhancement (CHEF).
  • A molecular 2:1 multiplexer was realized by using solvents to control inputs and report selectively.

Conclusions:

  • A simple molecular system effectively functions as a 2:1 multiplexer.
  • PET modulation via protonation and metal ion chelation is a viable strategy for molecular logic.
  • This work provides a foundation for developing sophisticated molecular information processing systems.