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

G-Protein Gated Ion Channels01:21

G-Protein Gated Ion Channels

6.9K
GPCRs are primarily responsible for our sense of smell, taste, and vision.  The binding of a sensory stimulus activates GPCR to stimulate effector proteins, many of which are ion channels in the sensory organs. GPCRs modulate the opening and closing of the target ion channels either directly by binding them, or by releasing second messengers that activate these channels. As ions move across the membrane, the membrane potential is altered, which induces an appropriate response.
Sensory...
6.9K
Multi-pass Transmembrane Proteins and β-barrels01:09

Multi-pass Transmembrane Proteins and β-barrels

6.8K
In multi-pass transmembrane proteins, the polypeptide chain crosses the membrane more than once. The transmembrane polypeptide chain either forms an α-helix or β-strand structure. α-Helix containing multi-pass transmembrane proteins are ubiquitous, whereas β-strand containing ones are mainly found in gram-negative bacteria, mitochondria, and chloroplasts.
α-Helix containing multi-pass transmembrane proteins
Multi-pass transmembrane proteins such as...
6.8K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

134.1K
G-protein coupled receptors are ligand binding receptors that indirectly affect changes in the cell. The actual receptor is a single polypeptide that transverses the cell membrane seven times creating intracellular and extracellular loops. The extracellular loops create a ligand specific pocket which binds to neurotransmitters or hormones. The intracellular loops holds onto the G-protein.
134.1K
G-protein Coupled Receptors01:21

G-protein Coupled Receptors

7.0K
7.0K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

19.5K
G Protein-Coupled Receptors or GPCRs are membrane-bound receptors that transiently associate with heterotrimeric G proteins and induce an appropriate response to sensory stimuli such as light, odors, hormones, cytokines, or neurotransmitters.
GPCRs are also called heptahelical, 7TM, or serpentine receptors, and consist of seven (H1-H7) transmembrane alpha-helices that span the bilayer to form a cylindrical core. The transmembrane helices are connected by three extracellular loops and three...
19.5K
G Protein-coupled Receptors01:15

G Protein-coupled Receptors

2.5K
2.5K

You might also read

Related Articles

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

Sort by
Same author

Protonation State-dependent Interaction of Polycationic Polymyxins with the <i>Pseudomonas aeruginosa</i> Outer Membrane Using Colistin A as a Model.

Journal of chemical information and modeling·2026
Same author

Retargeting Gram-Positive-Only Adarotene-Derived Antibacterials to Broad-Spectrum Antibiotics.

Antibiotics (Basel, Switzerland)·2025
Same author

Bile acids in liver and gastrointestinal cancer.

Seminars in cancer biology·2025
Same author

Regiodivergence in the Cycloadditions between a Cyclic Nitrone and Carbonyl-Type Dipolarophiles.

The Journal of organic chemistry·2025
Same author

Gut-to-bile transfer of microbially amidated minor bile acids in patients with hepatopancreatobiliary disorders.

Hepatology (Baltimore, Md.)·2025
Same author

A novel noninvasive test based on near-infrared fluorescent cholephilic probes for hepatobiliary secretory function assessment.

Biomedicine & pharmacotherapy = Biomedecine & pharmacotherapie·2025

Related Experiment Video

Updated: Mar 28, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.6K

A highly selective receptor for zwitterionic proline.

Álvaro G Temprano1, Laura M Monleón, Omayra H Rubio

  • 1Organic Chemistry Department, Plaza de los Caidos 1-5, University of Salamanca, 37008 Salamanca, Spain. romoran@usal.es.

Organic & Biomolecular Chemistry
|December 15, 2015
PubMed
Summary

Researchers developed a chiral receptor mimicking enzyme active sites for selective proline extraction. This receptor enables enantioselective separation of L-proline from racemic mixtures using H-bonds and cation-π interactions.

More Related Videos

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K
Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
16:16

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

15.9K

Related Experiment Videos

Last Updated: Mar 28, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

3.6K
Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions
06:50

Author Spotlight: A Computational Approach to Decipher Amino Acid Preferences in Multispecific Protein-Protein Interactions

Published on: January 26, 2024

2.7K
Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors
16:16

Genetically-encoded Molecular Probes to Study G Protein-coupled Receptors

Published on: September 13, 2013

15.9K

Area of Science:

  • Supramolecular Chemistry
  • Organic Synthesis
  • Chiral Recognition

Background:

  • Enzymes utilize specific active site motifs, like the oxyanion hole, for substrate binding and catalysis.
  • Developing synthetic receptors that mimic these enzymatic functions is crucial for understanding molecular recognition.
  • Selective extraction of amino acids, particularly proline, presents challenges due to their zwitterionic nature.

Purpose of the Study:

  • To synthesize a novel chiral chromane receptor designed to mimic the oxyanion hole of enzymes.
  • To investigate the receptor's ability to form host-guest complexes with zwitterionic proline via hydrogen bonds and cation-π interactions.
  • To achieve enantioselective extraction of proline from aqueous solutions.

Main Methods:

  • Synthesis of a chiral chromane receptor.
  • Host-guest complexation studies with proline and other amino acids.
  • Enantioselective extraction experiments using a chloroform phase.
  • Spectroscopic analyses (NOE, CD) and X-ray diffraction for structural elucidation and configuration determination.
  • Molecular modeling studies.

Main Results:

  • A chiral chromane receptor successfully mimicked the enzyme oxyanion hole.
  • The receptor formed a selective host-guest complex with zwitterionic proline, enabling its extraction into a chloroform phase, excluding other amino acids.
  • Enantioselective extraction of proline was achieved due to the receptor's chirality.
  • L-Proline was used to resolve the receptor's racemic mixture, and its absolute configuration was determined.

Conclusions:

  • The synthesized chiral chromane receptor effectively mimics enzymatic oxyanion holes for selective guest binding.
  • The combination of H-bonds and cation-π interactions facilitates the recognition and extraction of proline.
  • This study demonstrates a novel method for enantioselective proline separation and receptor configuration determination.